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Chlorine in PDB 1qh1: Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State

Enzymatic activity of Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State

All present enzymatic activity of Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State:
1.18.6.1;

Protein crystallography data

The structure of Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State, PDB code: 1qh1 was solved by S.M.Mayer, D.M.Lawson, C.A.Gormal, S.M.Roe, B.E.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 204.180, 75.220, 162.840, 90.00, 122.88, 90.00
R / Rfree (%) 15.8 / 19.9

Other elements in 1qh1:

The structure of Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State also contains other interesting chemical elements:

Molybdenum (Mo) 2 atoms
Magnesium (Mg) 7 atoms
Iron (Fe) 30 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State (pdb code 1qh1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State, PDB code: 1qh1:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1qh1

Go back to Chlorine Binding Sites List in 1qh1
Chlorine binding site 1 out of 2 in the Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl2771

b:20.6
occ:1.00
O B:HOH3091 3.1 19.3 1.0
O B:HOH3087 3.1 18.6 1.0
O B:HOH3041 3.3 15.9 1.0
N B:ASN395 3.5 16.7 1.0
CB B:TRP398 3.7 14.3 1.0
CB B:PRO369 3.8 13.7 1.0
CA B:ALA394 3.8 15.8 1.0
CG B:ASN395 3.9 18.0 1.0
OD1 B:ASN395 3.9 18.4 1.0
CG B:PRO369 3.9 13.2 1.0
ND2 B:ASN395 4.0 20.9 1.0
CE3 B:TRP292 4.1 17.7 1.0
CB B:TRP292 4.1 15.0 1.0
CG B:TRP398 4.1 13.4 1.0
C B:ALA394 4.1 16.6 1.0
O B:HOH3181 4.2 24.1 1.0
CD1 B:TRP398 4.3 13.5 1.0
CB B:ALA394 4.3 16.0 1.0
CB B:ASN395 4.4 16.1 1.0
O B:ASN393 4.5 16.9 1.0
CA B:ASN395 4.6 17.8 1.0
O B:TRP292 4.6 18.1 1.0
CD2 B:TRP292 4.6 15.3 1.0
CG B:TRP292 4.7 13.3 1.0
O B:HOH3403 4.8 36.4 1.0
CZ3 B:TRP292 4.9 17.2 1.0
N B:ALA394 5.0 14.2 1.0

Chlorine binding site 2 out of 2 in 1qh1

Go back to Chlorine Binding Sites List in 1qh1
Chlorine binding site 2 out of 2 in the Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl2772

b:17.1
occ:1.00
O D:HOH3109 3.1 19.0 1.0
O D:HOH3089 3.1 16.8 1.0
O D:HOH3048 3.3 13.8 1.0
N D:ASN395 3.5 14.3 1.0
CB D:TRP398 3.7 13.5 1.0
CB D:PRO369 3.7 12.5 1.0
CA D:ALA394 3.8 12.8 1.0
OD1 D:ASN395 3.8 15.7 1.0
CG D:ASN395 3.9 19.3 1.0
CG D:PRO369 3.9 12.2 1.0
CG D:TRP398 4.1 13.3 1.0
C D:ALA394 4.1 16.4 1.0
ND2 D:ASN395 4.1 17.7 1.0
CB D:TRP292 4.1 13.2 1.0
O D:HOH3161 4.2 21.4 1.0
CE3 D:TRP292 4.2 14.5 1.0
CD1 D:TRP398 4.2 16.8 1.0
CB D:ALA394 4.2 13.7 1.0
CB D:ASN395 4.4 15.4 1.0
CA D:ASN395 4.5 16.8 1.0
O D:ASN393 4.6 16.6 1.0
O D:TRP292 4.7 15.8 1.0
CD2 D:TRP292 4.7 14.7 1.0
CG D:TRP292 4.7 10.8 1.0
O D:HOH3352 4.9 31.6 1.0
N D:ALA394 4.9 11.4 1.0
CA D:TRP398 5.0 15.3 1.0

Reference:

S.M.Mayer, D.M.Lawson, C.A.Gormal, S.M.Roe, B.E.Smith. New Insights Into Structure-Function Relationships in Nitrogenase: A 1.6 A Resolution X-Ray Crystallographic Study of Klebsiella Pneumoniae Mofe-Protein. J.Mol.Biol. V. 292 871 1999.
ISSN: ISSN 0022-2836
PubMed: 10525412
DOI: 10.1006/JMBI.1999.3107
Page generated: Sat Dec 12 08:46:58 2020

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