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Chlorine in PDB 2qd4: Wild Type Human Ferrochelatase Crystallized with MNCL2

Enzymatic activity of Wild Type Human Ferrochelatase Crystallized with MNCL2

All present enzymatic activity of Wild Type Human Ferrochelatase Crystallized with MNCL2:
4.99.1.1;

Protein crystallography data

The structure of Wild Type Human Ferrochelatase Crystallized with MNCL2, PDB code: 2qd4 was solved by A.E.Medlock, T.A.Dailey, T.A.Ross, H.A.Dailey, W.N.Lanzilotta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.85 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 87.586, 93.062, 109.980, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 23

Other elements in 2qd4:

The structure of Wild Type Human Ferrochelatase Crystallized with MNCL2 also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Wild Type Human Ferrochelatase Crystallized with MNCL2 (pdb code 2qd4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the Wild Type Human Ferrochelatase Crystallized with MNCL2, PDB code: 2qd4:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in 2qd4

Go back to Chlorine Binding Sites List in 2qd4
Chlorine binding site 1 out of 6 in the Wild Type Human Ferrochelatase Crystallized with MNCL2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Wild Type Human Ferrochelatase Crystallized with MNCL2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl701

b:33.7
occ:1.00
 OH A:TYR123 3.0 21.9 1.0
O A:HOH912 3.1 33.1 1.0
OG A:SER130 3.1 22.0 1.0
N A:ILE342 3.1 19.8 1.0
CB A:HIS341 3.3 19.9 1.0
CB A:SER130 3.4 21.1 1.0
CD1 A:ILE132 3.6 21.4 1.0
CE2 A:TYR123 3.7 21.7 1.0
CA A:HIS341 3.8 19.7 1.0
CB A:ILE342 3.8 20.0 1.0
CZ A:TYR123 3.8 21.9 1.0
C A:HIS341 4.0 19.6 1.0
CG2 A:ILE342 4.0 20.5 1.0
CA A:ILE342 4.1 20.0 1.0
CA A:GLY78 4.1 21.4 1.0
CG1 A:ILE132 4.2 20.8 1.0
CA A:SER130 4.4 20.8 1.0
CG A:HIS341 4.4 20.2 1.0
O A:HOH999 4.6 36.5 1.0
ND1 A:HIS341 4.7 20.3 1.0
N A:GLY78 4.9 21.2 1.0
O A:GLY77 5.0 20.8 1.0

Chlorine binding site 2 out of 6 in 2qd4

Go back to Chlorine Binding Sites List in 2qd4
Chlorine binding site 2 out of 6 in the Wild Type Human Ferrochelatase Crystallized with MNCL2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Wild Type Human Ferrochelatase Crystallized with MNCL2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl703

b:39.5
occ:1.00
 O A:HOH965 2.8 25.5 1.0
N A:GLN398 3.1 17.5 1.0
O B:HOH957 3.2 19.5 1.0
O A:HOH1008 3.2 34.4 1.0
N A:LYS397 3.3 17.9 1.0
CG A:GLN398 3.5 16.9 1.0
CB A:LYS397 3.5 18.5 1.0
CD1 B:TYR793 3.7 22.3 1.0
CB B:TYR793 3.7 21.4 1.0
CA A:LYS397 3.8 18.0 1.0
CB A:GLN398 3.8 17.4 1.0
CG B:TYR793 3.8 22.1 1.0
CB A:SER396 3.8 17.6 1.0
C A:LYS397 3.9 17.8 1.0
CA A:GLN398 4.0 17.4 1.0
C A:SER396 4.2 17.8 1.0
OG A:SER396 4.2 16.6 1.0
CA A:SER396 4.4 17.8 1.0
CD A:GLN398 4.5 17.2 1.0
OE1 A:GLN398 4.5 17.1 1.0
CE1 B:TYR793 4.5 22.8 1.0
CG A:LYS397 4.6 19.1 1.0
CD2 B:TYR793 4.7 22.4 1.0
CA B:TYR793 5.0 20.9 1.0
O B:TYR793 5.0 20.1 1.0

Chlorine binding site 3 out of 6 in 2qd4

Go back to Chlorine Binding Sites List in 2qd4
Chlorine binding site 3 out of 6 in the Wild Type Human Ferrochelatase Crystallized with MNCL2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Wild Type Human Ferrochelatase Crystallized with MNCL2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl705

b:46.0
occ:1.00
 NH1 B:ARG827 3.0 23.3 1.0
O A:HOH820 3.2 31.9 1.0
N A:SER402 3.2 20.6 1.0
CD B:ARG827 3.7 23.4 1.0
CG B:ARG827 3.8 23.5 1.0
O A:THR400 3.8 19.1 1.0
CA A:LEU401 3.9 19.8 1.0
CB A:SER402 3.9 21.7 1.0
CD1 A:LEU401 4.0 19.3 1.0
CZ B:ARG827 4.1 23.7 1.0
C A:LEU401 4.1 20.2 1.0
OG A:SER402 4.1 23.0 1.0
CA A:SER402 4.2 21.1 1.0
CE A:LYS415 4.2 27.8 1.0
O A:HOH996 4.3 43.1 1.0
NE B:ARG827 4.3 23.7 1.0
O A:SER402 4.6 20.8 1.0
C A:THR400 4.6 19.1 1.0
N A:LEU401 4.7 19.3 1.0
O B:HOH1140 4.7 40.5 1.0
C A:SER402 4.8 20.9 1.0
CB A:LEU401 4.9 19.6 1.0
O A:HOH1020 4.9 40.4 1.0
CD A:LYS415 4.9 27.4 1.0
CG A:LEU401 5.0 19.6 1.0

Chlorine binding site 4 out of 6 in 2qd4

Go back to Chlorine Binding Sites List in 2qd4
Chlorine binding site 4 out of 6 in the Wild Type Human Ferrochelatase Crystallized with MNCL2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Wild Type Human Ferrochelatase Crystallized with MNCL2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl706

b:46.0
occ:1.00
 NH1 A:ARG327 2.9 24.3 1.0
O B:HOH966 3.1 29.9 1.0
N B:SER902 3.2 20.5 1.0
CD A:ARG327 3.7 24.9 1.0
CG A:ARG327 3.8 24.7 1.0
CB B:SER902 3.8 21.7 1.0
OG B:SER902 3.9 22.5 1.0
O B:THR900 3.9 19.1 1.0
CD1 B:LEU901 4.0 20.0 1.0
CA B:LEU901 4.0 20.0 1.0
CZ A:ARG327 4.1 24.9 1.0
CA B:SER902 4.1 21.1 1.0
C B:LEU901 4.1 20.3 1.0
NE A:ARG327 4.3 25.1 1.0
O B:HOH1048 4.4 44.6 1.0
O B:SER902 4.5 20.9 1.0
CE B:LYS915 4.5 28.6 1.0
C B:SER902 4.7 21.0 1.0
C B:THR900 4.7 19.2 1.0
N B:LEU901 4.8 19.5 1.0
O A:HOH917 4.9 33.2 1.0
CG B:LEU901 5.0 20.1 1.0
CB B:LEU901 5.0 19.7 1.0

Chlorine binding site 5 out of 6 in 2qd4

Go back to Chlorine Binding Sites List in 2qd4
Chlorine binding site 5 out of 6 in the Wild Type Human Ferrochelatase Crystallized with MNCL2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Wild Type Human Ferrochelatase Crystallized with MNCL2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl924

b:32.1
occ:1.00
 O B:HOH1031 3.0 33.7 1.0
OH B:TYR623 3.1 22.8 1.0
N B:ILE842 3.1 20.9 1.0
OG B:SER630 3.2 22.8 1.0
CB B:HIS841 3.3 21.1 1.0
CB B:SER630 3.4 22.3 1.0
CE2 B:TYR623 3.6 22.9 1.0
CD1 B:ILE632 3.7 22.1 1.0
CA B:HIS841 3.7 21.0 1.0
CZ B:TYR623 3.8 23.1 1.0
CB B:ILE842 3.8 21.4 1.0
C B:HIS841 3.9 20.8 1.0
CG2 B:ILE842 4.0 21.6 1.0
CA B:ILE842 4.0 21.2 1.0
CA B:GLY578 4.2 22.6 1.0
CG1 B:ILE632 4.2 21.8 1.0
CA B:SER630 4.4 22.3 1.0
CG B:HIS841 4.5 21.4 1.0
O B:HOH1039 4.6 33.4 1.0
ND1 B:HIS841 4.9 21.6 1.0
CD2 B:TYR623 4.9 23.1 1.0

Chlorine binding site 6 out of 6 in 2qd4

Go back to Chlorine Binding Sites List in 2qd4
Chlorine binding site 6 out of 6 in the Wild Type Human Ferrochelatase Crystallized with MNCL2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Wild Type Human Ferrochelatase Crystallized with MNCL2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl925

b:42.5
occ:1.00
 O B:HOH1029 2.9 30.6 1.0
N B:GLN898 3.1 17.2 1.0
O A:HOH869 3.1 20.0 1.0
N B:LYS897 3.2 18.0 1.0
O A:HOH966 3.3 32.3 1.0
CB B:LYS897 3.4 18.3 1.0
CG B:GLN898 3.5 16.9 1.0
CD1 A:TYR293 3.7 22.6 1.0
CA B:LYS897 3.7 17.9 1.0
CB A:TYR293 3.7 21.8 1.0
CB B:GLN898 3.7 17.3 1.0
CG A:TYR293 3.8 22.4 1.0
CB B:SER896 3.8 18.2 1.0
C B:LYS897 3.8 17.6 1.0
CA B:GLN898 3.9 17.3 1.0
C B:SER896 4.1 18.1 1.0
OG B:SER896 4.1 17.9 1.0
CA B:SER896 4.4 18.4 1.0
CD B:GLN898 4.5 16.9 1.0
CG B:LYS897 4.5 18.8 1.0
CE1 A:TYR293 4.6 23.2 1.0
OE1 B:GLN898 4.6 16.7 1.0
CD2 A:TYR293 4.7 22.6 1.0
O A:HOH967 4.8 36.7 1.0
O B:HOH1132 4.9 40.6 1.0
CA A:TYR293 5.0 21.2 1.0
O B:LYS897 5.0 17.5 1.0

Reference:

A.E.Medlock, T.A.Dailey, T.A.Ross, H.A.Dailey, W.N.Lanzilotta. A Pi-Helix Switch Selective For Porphyrin Deprotonation and Product Release in Human Ferrochelatase. J.Mol.Biol. V. 373 1006 2007.
ISSN: ISSN 0022-2836
PubMed: 17884090
DOI: 10.1016/J.JMB.2007.08.040
Page generated: Sat Dec 12 09:16:49 2020

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