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Chlorine in PDB 6wng: Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1

Enzymatic activity of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1

All present enzymatic activity of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1:
4.3.1.1;

Protein crystallography data

The structure of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1, PDB code: 6wng was solved by Seattle Structural Genomics Center For Infectious Disease, Seattlestructural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.06 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 92.820, 96.850, 212.200, 90.00, 90.00, 90.00
R / Rfree (%) 13.4 / 15.3

Chlorine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Chlorine atom in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 (pdb code 6wng). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 12 binding sites of Chlorine where determined in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1, PDB code: 6wng:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 12 in 6wng

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Chlorine binding site 1 out of 12 in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl504

b:18.9
occ:1.00
OE2 D:GLU340 2.9 18.6 1.0
O C:HOH770 3.0 11.7 1.0
NH1 D:ARG305 3.0 12.4 1.0
CA A:GLN197 3.3 12.6 1.0
O A:GLN197 3.3 13.9 1.0
C A:GLN197 3.5 12.4 1.0
CD D:ARG305 3.6 10.1 1.0
CB A:GLN197 3.7 11.4 1.0
CD D:GLU340 3.7 18.8 1.0
CG D:GLU340 3.7 12.3 1.0
CG D:PRO336 3.8 10.4 1.0
CG2 C:VAL369 3.8 10.6 1.0
CG1 C:VAL369 4.0 13.6 1.0
CZ D:ARG305 4.0 11.3 1.0
NE D:ARG305 4.2 10.5 1.0
CG D:ARG305 4.4 12.4 1.0
CB D:ARG305 4.4 12.0 1.0
CB C:VAL369 4.4 9.9 1.0
N A:LEU198 4.4 11.3 1.0
OE1 C:GLN364 4.4 13.2 1.0
CD D:PRO336 4.5 12.2 1.0
N A:GLN197 4.6 10.6 1.0
CG A:GLN197 4.8 12.2 1.0
OE1 D:GLU340 4.8 14.9 1.0
CG A:LEU198 4.8 11.3 1.0
NE2 A:GLN197 4.9 11.8 1.0
O C:HOH828 4.9 11.7 1.0

Chlorine binding site 2 out of 12 in 6wng

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Chlorine binding site 2 out of 12 in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl505

b:23.4
occ:1.00
O A:HOH778 3.1 14.2 1.0
NZ A:LYS386 3.1 18.3 1.0
O A:HOH1043 3.5 30.3 1.0
NE A:ARG383 3.5 42.4 1.0
CB A:ARG383 3.9 11.7 1.0
CA A:ARG383 3.9 10.3 1.0
CE A:LYS386 4.0 21.5 1.0
CD A:LYS386 4.1 17.6 1.0
CD2 A:LEU165 4.1 11.7 1.0
CG A:ARG383 4.1 19.2 1.0
NH2 A:ARG383 4.2 35.6 1.0
N A:ARG383 4.2 9.0 1.0
O A:HOH706 4.3 16.8 1.0
CZ A:ARG383 4.3 46.0 1.0
CG2 A:ILE382 4.4 8.8 1.0
CD A:ARG383 4.4 31.7 1.0
O A:HOH889 4.4 34.9 1.0
O A:HOH1053 4.7 47.2 1.0
C A:ILE382 4.8 10.8 1.0
O A:HOH757 4.8 33.7 1.0

Chlorine binding site 3 out of 12 in 6wng

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Chlorine binding site 3 out of 12 in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl506

b:19.2
occ:1.00
O A:HOH1043 2.9 30.3 1.0
O A:HOH706 2.9 16.8 1.0
N A:GLU53 3.2 11.5 1.0
C A:HIS51 3.4 9.4 1.0
N A:PRO52 3.4 10.2 1.0
CA A:HIS51 3.4 10.7 1.0
CD A:PRO52 3.5 10.6 1.0
CB A:GLU53 3.6 11.6 1.0
CB A:HIS51 3.9 10.6 1.0
CG A:GLU53 3.9 13.7 1.0
CD2 A:LEU165 3.9 11.7 1.0
CA A:GLU53 3.9 12.5 1.0
CG A:PRO52 4.0 15.1 1.0
O A:HIS51 4.0 10.1 1.0
C A:PRO52 4.1 12.9 1.0
NH2 A:ARG383 4.2 35.6 1.0
CD1 A:LEU165 4.2 11.7 1.0
CA A:PRO52 4.3 11.6 1.0
N A:PHE54 4.3 10.0 1.0
ND1 A:HIS51 4.3 12.2 1.0
CG A:LEU165 4.5 11.4 1.0
CG A:HIS51 4.5 10.1 1.0
C A:GLU53 4.6 11.1 1.0
N A:HIS51 4.7 11.6 1.0
O A:ASP50 4.8 12.7 1.0
CB A:PRO52 4.8 14.1 1.0
O A:HOH1050 4.9 41.0 1.0
O A:HOH1053 5.0 47.2 1.0

Chlorine binding site 4 out of 12 in 6wng

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Chlorine binding site 4 out of 12 in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl504

b:16.6
occ:1.00
OE2 C:GLU340 2.9 16.9 1.0
NH1 C:ARG305 3.0 10.6 1.0
O D:HOH655 3.0 10.4 1.0
CA B:GLN197 3.3 9.0 1.0
O B:GLN197 3.4 12.0 1.0
C B:GLN197 3.5 11.4 1.0
CD C:ARG305 3.6 10.8 1.0
CD C:GLU340 3.7 16.8 1.0
CB B:GLN197 3.7 10.1 1.0
CG C:GLU340 3.7 9.6 1.0
CG C:PRO336 3.8 9.7 1.0
CG2 D:VAL369 3.9 9.5 1.0
CG1 D:VAL369 3.9 9.2 1.0
CZ C:ARG305 4.0 11.8 1.0
NE C:ARG305 4.1 10.7 1.0
CG C:ARG305 4.4 8.8 1.0
CB D:VAL369 4.4 8.6 1.0
CB C:ARG305 4.4 8.7 1.0
N B:LEU198 4.4 8.2 1.0
OE1 D:GLN364 4.4 10.7 1.0
CD C:PRO336 4.5 10.1 1.0
N B:GLN197 4.6 8.5 1.0
CG B:GLN197 4.7 11.5 1.0
OE1 C:GLU340 4.8 12.5 1.0
CG B:LEU198 4.9 8.9 1.0
O D:HOH795 4.9 10.2 1.0
NE2 B:GLN197 4.9 10.3 1.0

Chlorine binding site 5 out of 12 in 6wng

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Chlorine binding site 5 out of 12 in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl505

b:21.5
occ:1.00
O B:HOH837 3.1 15.5 1.0
NZ B:LYS386 3.2 19.3 1.0
O B:HOH1047 3.2 28.5 1.0
O B:HOH1082 3.4 35.5 1.0
NE B:ARG383 3.6 28.5 1.0
CB B:ARG383 3.8 11.7 1.0
CA B:ARG383 3.9 9.3 1.0
CD2 B:LEU165 4.1 13.7 1.0
CG B:ARG383 4.1 20.8 1.0
O B:HOH1002 4.1 47.8 1.0
CE B:LYS386 4.1 27.6 1.0
O B:HOH771 4.2 19.2 1.0
CD B:LYS386 4.2 18.1 1.0
NH2 B:ARG383 4.2 29.4 1.0
N B:ARG383 4.2 10.3 1.0
CZ B:ARG383 4.4 36.5 1.0
CD B:ARG383 4.4 24.3 1.0
CG2 B:ILE382 4.4 10.3 1.0
O B:HOH685 4.8 49.5 1.0
C B:ILE382 4.8 12.1 1.0

Chlorine binding site 6 out of 12 in 6wng

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Chlorine binding site 6 out of 12 in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl506

b:21.5
occ:1.00
O B:HOH771 3.0 19.2 1.0
O B:HOH1047 3.1 28.5 1.0
N B:GLU53 3.1 12.2 1.0
C B:HIS51 3.3 15.3 1.0
N B:PRO52 3.4 13.9 1.0
CA B:HIS51 3.4 12.8 1.0
CD B:PRO52 3.5 14.5 1.0
CB B:GLU53 3.5 13.0 1.0
CG B:GLU53 3.8 16.8 1.0
CB B:HIS51 3.8 11.8 1.0
CA B:GLU53 3.9 12.2 1.0
CD2 B:LEU165 3.9 13.7 1.0
O B:HIS51 3.9 13.8 1.0
CG B:PRO52 4.0 16.1 1.0
C B:PRO52 4.1 14.3 1.0
CD1 B:LEU165 4.2 14.2 1.0
N B:PHE54 4.2 12.5 1.0
CA B:PRO52 4.2 11.9 1.0
ND1 B:HIS51 4.3 14.2 1.0
CG B:LEU165 4.5 13.2 1.0
NH2 B:ARG383 4.5 29.4 1.0
CG B:HIS51 4.5 12.6 1.0
C B:GLU53 4.5 13.1 1.0
N B:HIS51 4.7 12.7 1.0
CB B:PRO52 4.8 13.3 1.0
O B:ASP50 4.8 14.6 1.0

Chlorine binding site 7 out of 12 in 6wng

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Chlorine binding site 7 out of 12 in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl604

b:16.3
occ:1.00
OE2 B:GLU340 2.9 14.5 1.0
O A:HOH676 3.0 10.2 1.0
NH1 B:ARG305 3.0 11.0 1.0
CA C:GLN197 3.3 8.3 1.0
O C:GLN197 3.3 10.2 1.0
C C:GLN197 3.5 9.8 1.0
CD B:ARG305 3.6 9.0 1.0
CB C:GLN197 3.7 8.8 1.0
CD B:GLU340 3.7 13.4 1.0
CG B:GLU340 3.8 12.1 1.0
CG B:PRO336 3.8 9.3 1.0
CG2 A:VAL369 3.9 9.2 1.0
CZ B:ARG305 4.0 10.0 1.0
CG1 A:VAL369 4.0 9.9 1.0
NE B:ARG305 4.2 9.9 1.0
CG B:ARG305 4.4 8.9 1.0
CB B:ARG305 4.4 7.8 1.0
OE1 A:GLN364 4.4 10.6 1.0
N C:LEU198 4.4 8.5 1.0
CB A:VAL369 4.4 9.2 1.0
CD B:PRO336 4.4 11.8 1.0
N C:GLN197 4.6 8.1 1.0
CG C:LEU198 4.8 9.2 1.0
CG C:GLN197 4.8 9.8 1.0
OE1 B:GLU340 4.8 11.4 1.0
NE2 C:GLN197 4.9 8.6 1.0
O A:HOH738 4.9 9.6 1.0

Chlorine binding site 8 out of 12 in 6wng

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Chlorine binding site 8 out of 12 in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl605

b:21.9
occ:1.00
O C:HOH934 3.1 14.5 1.0
O C:HOH1135 3.1 36.9 1.0
NZ C:LYS386 3.2 17.2 1.0
O C:HOH1148 3.3 32.2 1.0
NE C:ARG383 3.5 29.1 1.0
CB C:ARG383 3.7 14.6 1.0
CA C:ARG383 3.9 10.4 1.0
CG C:ARG383 4.0 20.8 1.0
CE C:LYS386 4.0 19.8 1.0
CD2 C:LEU165 4.1 13.8 1.0
NH2 C:ARG383 4.2 29.6 1.0
CD C:LYS386 4.2 18.9 1.0
O C:HOH832 4.3 19.3 1.0
N C:ARG383 4.3 10.7 1.0
CZ C:ARG383 4.3 36.7 1.0
CD C:ARG383 4.3 25.8 1.0
CG2 C:ILE382 4.5 10.4 1.0
O C:HOH762 4.8 47.6 1.0
C C:ILE382 4.8 10.9 1.0

Chlorine binding site 9 out of 12 in 6wng

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Chlorine binding site 9 out of 12 in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl606

b:20.6
occ:1.00
O C:HOH832 3.0 19.3 1.0
O C:HOH1148 3.0 32.2 1.0
N C:GLU53 3.2 14.5 1.0
C C:HIS51 3.4 14.2 1.0
N C:PRO52 3.4 13.2 1.0
CA C:HIS51 3.4 13.2 1.0
CD C:PRO52 3.5 13.8 1.0
CB C:GLU53 3.6 15.2 1.0
CG C:GLU53 3.8 17.7 1.0
CB C:HIS51 3.8 12.3 1.0
CA C:GLU53 3.9 13.2 1.0
CD2 C:LEU165 3.9 13.8 1.0
O C:HIS51 4.0 12.5 1.0
CG C:PRO52 4.0 14.2 1.0
C C:PRO52 4.1 16.4 1.0
CD1 C:LEU165 4.2 13.2 1.0
N C:PHE54 4.2 14.5 1.0
NH2 C:ARG383 4.2 29.6 1.0
CA C:PRO52 4.3 14.2 1.0
ND1 C:HIS51 4.4 13.1 1.0
CG C:LEU165 4.5 10.3 1.0
CG C:HIS51 4.6 11.5 1.0
C C:GLU53 4.6 16.1 1.0
N C:HIS51 4.8 12.8 1.0
CB C:PRO52 4.8 14.7 1.0
O C:HOH1142 4.8 35.4 1.0
O C:ASP50 4.8 16.4 1.0

Chlorine binding site 10 out of 12 in 6wng

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Chlorine binding site 10 out of 12 in the Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl504

b:18.1
occ:1.00
OE2 A:GLU340 3.0 18.8 1.0
NH1 A:ARG305 3.0 12.1 1.0
O B:HOH656 3.0 12.2 1.0
CA D:GLN197 3.3 10.3 1.0
O D:GLN197 3.3 12.7 1.0
C D:GLN197 3.5 11.7 1.0
CD A:ARG305 3.6 10.2 1.0
CB D:GLN197 3.7 11.7 1.0
CD A:GLU340 3.7 17.1 1.0
CG A:GLU340 3.7 11.5 1.0
CG A:PRO336 3.8 11.1 1.0
CG2 B:VAL369 3.9 14.3 1.0
CG1 B:VAL369 3.9 11.0 1.0
CZ A:ARG305 3.9 10.8 1.0
NE A:ARG305 4.1 10.5 1.0
CG A:ARG305 4.4 10.4 1.0
CB A:ARG305 4.4 11.6 1.0
CB B:VAL369 4.4 10.9 1.0
OE1 B:GLN364 4.4 12.3 1.0
N D:LEU198 4.4 12.1 1.0
CD A:PRO336 4.5 12.1 1.0
N D:GLN197 4.6 10.7 1.0
CG D:GLN197 4.7 13.5 1.0
OE1 A:GLU340 4.8 13.5 1.0
CG D:LEU198 4.8 12.6 1.0
NE2 D:GLN197 4.9 12.2 1.0
O B:HOH726 4.9 11.8 1.0

Reference:

T.E.Edwards, S.J.Mayclin, J.Abendroth, P.S.Horanyi, D.D.Lorimer, Seattle Structural Genomics Center For Infectious Disease. Crystal Structure of An Aspartate Ammonia-Lyase From Elizabethkingia Anophelis NUHP1 To Be Published.
Page generated: Mon Jul 29 16:48:16 2024

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