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Chlorine in PDB 5bvh: Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii

Enzymatic activity of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii

All present enzymatic activity of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii:
1.18.6.1;

Protein crystallography data

The structure of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii, PDB code: 5bvh was solved by T.Spatzal, K.A.Perez, J.B.Howard, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.43 / 1.53
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 81.071, 130.833, 107.318, 90.00, 110.64, 90.00
R / Rfree (%) 14.4 / 16

Other elements in 5bvh:

The structure of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii also contains other interesting chemical elements:

Molybdenum (Mo) 4 atoms
Iron (Fe) 46 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii (pdb code 5bvh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii, PDB code: 5bvh:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5bvh

Go back to Chlorine Binding Sites List in 5bvh
Chlorine binding site 1 out of 2 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl505

b:11.6
occ:0.75
O B:HOH1122 2.9 8.9 1.0
OG1 A:THR111 3.0 9.9 1.0
NH2 A:ARG93 3.3 9.3 1.0
CG B:PHE450 3.4 9.7 1.0
NH2 B:ARG453 3.7 10.1 0.5
O A:THR111 3.7 9.5 1.0
CB B:PHE450 3.7 9.3 1.0
NH1 B:ARG453 3.7 10.5 0.5
CD1 B:PHE450 3.8 10.7 1.0
C A:THR111 3.8 9.3 1.0
CB A:THR111 3.8 9.5 1.0
NH1 B:ARG453 3.8 12.0 0.5
CD2 B:PHE450 3.8 10.3 1.0
CG2 A:THR104 3.8 9.7 1.0
CG A:MET112 3.9 10.4 1.0
N A:MET112 4.1 9.3 1.0
CZ B:ARG453 4.1 10.4 0.5
CE2 B:PHE450 4.3 10.8 1.0
CE1 B:PHE450 4.3 10.9 1.0
CA A:THR111 4.4 9.3 1.0
CA A:MET112 4.4 9.4 1.0
CZ A:ARG93 4.5 8.7 1.0
CZ B:PHE450 4.6 11.1 1.0
O B:HOH779 4.7 16.0 1.0
NE A:ARG93 4.8 8.2 1.0
CB A:MET112 4.8 10.0 1.0
CB A:THR104 4.9 9.6 1.0
O A:HOH889 4.9 26.7 1.0
CZ B:ARG453 5.0 11.7 0.5

Chlorine binding site 2 out of 2 in 5bvh

Go back to Chlorine Binding Sites List in 5bvh
Chlorine binding site 2 out of 2 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl505

b:10.2
occ:0.75
O D:HOH1135 2.9 9.4 1.0
OG1 C:THR111 2.9 9.4 1.0
NH2 C:ARG93 3.3 8.7 1.0
CG D:PHE450 3.4 9.7 1.0
NH2 D:ARG453 3.7 18.4 0.5
CB D:PHE450 3.7 9.4 1.0
O C:THR111 3.7 8.7 1.0
CG2 C:THR104 3.7 9.2 1.0
NH1 D:ARG453 3.7 11.3 0.5
NH2 D:ARG453 3.7 10.1 0.5
C C:THR111 3.7 9.1 1.0
CD2 D:PHE450 3.8 10.1 1.0
CD1 D:PHE450 3.8 10.3 1.0
CB C:THR111 3.8 9.3 1.0
CG C:MET112 3.9 10.3 1.0
N C:MET112 4.1 9.0 1.0
CZ D:ARG453 4.2 10.1 0.5
CE2 D:PHE450 4.3 10.6 1.0
CE1 D:PHE450 4.3 10.8 1.0
CA C:THR111 4.3 9.0 1.0
CA C:MET112 4.4 9.4 1.0
CZ C:ARG93 4.5 8.4 1.0
CZ D:PHE450 4.5 10.8 1.0
O D:HOH831 4.7 17.4 1.0
O D:HOH710 4.8 25.6 1.0
NE C:ARG93 4.8 8.1 1.0
CB C:MET112 4.8 9.9 1.0
CB C:THR104 4.8 9.2 1.0
CZ D:ARG453 4.9 16.2 0.5
ND2 D:ASN65 5.0 8.5 1.0

Reference:

T.Spatzal, K.A.Perez, J.B.Howard, D.C.Rees. Catalysis-Dependent Selenium Incorporation and Migration in the Nitrogenase Active Site Iron-Molybdenum Cofactor. Elife V. 4 11620 2015.
ISSN: ESSN 2050-084X
PubMed: 26673079
DOI: 10.7554/ELIFE.11620
Page generated: Sat Jul 12 00:34:07 2025

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