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Chlorine in PDB 5bvg: Selenium Incorporated Nitrogenase Mofe-Protein (AV1-SE2B) From A. Vinelandii

Enzymatic activity of Selenium Incorporated Nitrogenase Mofe-Protein (AV1-SE2B) From A. Vinelandii

All present enzymatic activity of Selenium Incorporated Nitrogenase Mofe-Protein (AV1-SE2B) From A. Vinelandii:
1.18.6.1;

Protein crystallography data

The structure of Selenium Incorporated Nitrogenase Mofe-Protein (AV1-SE2B) From A. Vinelandii, PDB code: 5bvg 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) 101.38 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 77.582, 130.825, 107.128, 90.00, 108.85, 90.00
R / Rfree (%) 15.2 / 17.9

Other elements in 5bvg:

The structure of Selenium Incorporated Nitrogenase Mofe-Protein (AV1-SE2B) From A. Vinelandii also contains other interesting chemical elements:

Molybdenum (Mo) 2 atoms
Iron (Fe) 32 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Selenium Incorporated Nitrogenase Mofe-Protein (AV1-SE2B) From A. Vinelandii (pdb code 5bvg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Selenium Incorporated Nitrogenase Mofe-Protein (AV1-SE2B) From A. Vinelandii, PDB code: 5bvg:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5bvg

Go back to Chlorine Binding Sites List in 5bvg
Chlorine binding site 1 out of 2 in the Selenium Incorporated Nitrogenase Mofe-Protein (AV1-SE2B) 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 Selenium Incorporated Nitrogenase Mofe-Protein (AV1-SE2B) From A. Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl504

b:13.9
occ:0.75
SE B:SE605 2.5 12.4 0.2
OG1 A:THR111 2.9 10.8 1.0
O B:HOH1033 3.0 16.5 0.8
NH2 A:ARG93 3.3 11.4 1.0
CG B:PHE450 3.4 11.0 1.0
CB B:PHE450 3.6 10.8 1.0
O A:THR111 3.7 10.2 1.0
CD1 B:PHE450 3.7 12.3 1.0
NH1 B:ARG453 3.7 10.2 0.5
CG2 A:THR104 3.7 11.7 1.0
C A:THR111 3.8 10.4 1.0
CD2 B:PHE450 3.8 11.0 1.0
CB A:THR111 3.8 9.6 1.0
NH2 B:ARG453 3.8 13.7 0.5
NH2 B:ARG453 3.9 12.4 0.5
CG A:MET112 3.9 12.1 1.0
N A:MET112 4.1 10.3 1.0
O B:HOH799 4.2 28.7 1.0
CZ B:ARG453 4.2 11.9 0.5
CE1 B:PHE450 4.3 13.1 1.0
CE2 B:PHE450 4.3 12.5 1.0
CA A:THR111 4.3 9.9 1.0
CA A:MET112 4.4 11.2 1.0
CZ A:ARG93 4.5 10.6 1.0
CZ B:PHE450 4.5 12.9 1.0
CB A:MET112 4.8 12.3 1.0
O B:HOH800 4.8 19.6 1.0
NE A:ARG93 4.8 9.5 1.0
CB A:THR104 4.9 11.7 1.0
ND2 B:ASN65 5.0 10.7 1.0

Chlorine binding site 2 out of 2 in 5bvg

Go back to Chlorine Binding Sites List in 5bvg
Chlorine binding site 2 out of 2 in the Selenium Incorporated Nitrogenase Mofe-Protein (AV1-SE2B) 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 Selenium Incorporated Nitrogenase Mofe-Protein (AV1-SE2B) From A. Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl504

b:13.3
occ:0.75
SE D:SE604 2.7 8.5 0.2
OG1 C:THR111 3.0 9.0 1.0
O D:HOH1049 3.0 18.9 0.8
NH2 C:ARG93 3.3 8.8 1.0
CG D:PHE450 3.4 9.7 1.0
CB D:PHE450 3.7 9.4 1.0
NH2 D:ARG453 3.7 13.2 0.6
CD1 D:PHE450 3.7 11.3 1.0
CG2 C:THR104 3.7 10.9 1.0
O C:THR111 3.7 8.9 1.0
CD2 D:PHE450 3.8 9.1 1.0
C C:THR111 3.8 8.4 1.0
CB C:THR111 3.8 7.9 1.0
NH1 D:ARG453 3.8 14.6 0.6
CG C:MET112 3.9 9.6 1.0
N C:MET112 4.1 8.0 1.0
CZ D:ARG453 4.2 12.6 0.6
CE1 D:PHE450 4.3 11.6 1.0
CE2 D:PHE450 4.3 10.2 1.0
CA C:THR111 4.4 8.1 1.0
CA C:MET112 4.4 8.3 1.0
CZ C:ARG93 4.5 8.7 1.0
CZ D:PHE450 4.5 11.4 1.0
O D:HOH705 4.6 22.8 1.0
O D:HOH896 4.7 18.0 1.0
CB C:THR104 4.8 10.2 1.0
CB C:MET112 4.8 8.9 1.0
NE C:ARG93 4.9 7.8 1.0
ND2 D:ASN65 4.9 7.8 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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