Chlorine in PDB 5v9j: Crystal Structure of Catalytic Domain of Glp with MS0105

Enzymatic activity of Crystal Structure of Catalytic Domain of Glp with MS0105

All present enzymatic activity of Crystal Structure of Catalytic Domain of Glp with MS0105:
2.1.1.43;

Protein crystallography data

The structure of Crystal Structure of Catalytic Domain of Glp with MS0105, PDB code: 5v9j was solved by A.Dong, H.Zeng, J.Liu, Y.Xiong, N.Babault, J.Jin, W.Tempel, C.Bountra, C.H.Arrowsmith, A.M.Edwards, H.Wu, P.J.Brown, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.74
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 74.848, 95.891, 102.416, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 19.7

Other elements in 5v9j:

The structure of Crystal Structure of Catalytic Domain of Glp with MS0105 also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Catalytic Domain of Glp with MS0105 (pdb code 5v9j). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Catalytic Domain of Glp with MS0105, PDB code: 5v9j:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 5v9j

Go back to Chlorine Binding Sites List in 5v9j
Chlorine binding site 1 out of 3 in the Crystal Structure of Catalytic Domain of Glp with MS0105


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 Catalytic Domain of Glp with MS0105 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1307

b:28.4
occ:1.00
ND2 A:ASN1122 3.1 15.3 1.0
NH2 A:ARG1125 3.2 16.6 1.0
O A:HOH1539 3.5 13.9 1.0
NE A:ARG1125 3.6 15.6 1.0
CA A:VAL1119 3.7 14.0 1.0
O A:ARG1118 3.7 16.9 1.0
CB A:ASN1122 3.8 15.1 1.0
O A:VAL1119 3.8 13.7 1.0
CZ A:ARG1125 3.8 16.0 1.0
O A:HOH1672 3.9 15.6 1.0
CG A:ASN1122 3.9 15.6 1.0
C A:VAL1119 4.2 13.7 1.0
CG1 A:VAL1119 4.3 14.9 1.0
CB A:VAL1119 4.3 14.2 1.0
CG2 A:VAL1119 4.4 14.6 1.0
C A:ARG1118 4.5 15.6 1.0
N A:VAL1119 4.5 14.6 1.0
CD A:ARG1125 4.8 15.3 1.0
O A:HOH1452 4.9 26.3 1.0

Chlorine binding site 2 out of 3 in 5v9j

Go back to Chlorine Binding Sites List in 5v9j
Chlorine binding site 2 out of 3 in the Crystal Structure of Catalytic Domain of Glp with MS0105


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 Catalytic Domain of Glp with MS0105 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1308

b:40.4
occ:1.00
O A:HOH1601 3.0 16.1 1.0
NH1 A:ARG1054 3.2 36.1 1.0
NH2 A:ARG1054 3.4 34.1 1.0
CZ A:ARG1054 3.8 33.4 1.0
O A:HOH1668 3.9 21.2 1.0
CD2 A:HIS1216 4.0 13.7 1.0
O A:HOH1640 4.2 24.2 1.0
NH1 A:ARG1223 4.3 14.0 1.0
CB A:ALA1215 4.3 14.6 1.0
NE2 A:HIS1216 4.6 13.8 1.0
O A:HOH1461 4.8 18.3 1.0
CD A:ARG1223 4.8 13.4 1.0
O A:HOH1561 5.0 18.7 1.0

Chlorine binding site 3 out of 3 in 5v9j

Go back to Chlorine Binding Sites List in 5v9j
Chlorine binding site 3 out of 3 in the Crystal Structure of Catalytic Domain of Glp with MS0105


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 Catalytic Domain of Glp with MS0105 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1307

b:40.4
occ:1.00
O B:HOH1596 3.0 14.4 1.0
NH1 B:ARG1054 3.3 34.1 1.0
NH2 B:ARG1054 3.3 33.5 1.0
CZ B:ARG1054 3.8 32.4 1.0
O B:HOH1673 3.9 25.2 1.0
CD2 B:HIS1216 3.9 16.4 1.0
O B:HOH1647 4.1 25.8 1.0
CB B:ALA1215 4.2 14.5 1.0
NH1 B:ARG1223 4.3 15.8 1.0
NE2 B:HIS1216 4.6 16.8 1.0
O B:HOH1458 4.8 22.6 1.0
O B:HOH1597 4.9 23.2 1.0
CD B:ARG1223 4.9 14.2 1.0
CG B:HIS1216 5.0 16.2 1.0

Reference:

H.Zeng, A.Dong, J.Liu, Y.Xiong, N.Babault, J.Jin, W.Tempel, C.Bountra, C.H.Arrowsmith, A.M.Edwards, H.Wu, P.J.Brown, Structural Genomics Consortium (Sgc). Crystal Structure of Catalytic Domain of Glp with MS0105 To Be Published.
Page generated: Sat Dec 12 12:33:39 2020

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