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Molybdenum in PDB 2a9b: Crystal Structure of R138Q Mutant of Recombinant Sulfite Oxidase at Resting State

Enzymatic activity of Crystal Structure of R138Q Mutant of Recombinant Sulfite Oxidase at Resting State

All present enzymatic activity of Crystal Structure of R138Q Mutant of Recombinant Sulfite Oxidase at Resting State:
1.8.3.1;

Protein crystallography data

The structure of Crystal Structure of R138Q Mutant of Recombinant Sulfite Oxidase at Resting State, PDB code: 2a9b was solved by E.Karakas, H.L.Wilson, T.N.Graf, S.Xiang, S.Jaramillo-Busquets, K.V.Rajagopalan, C.Kisker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.50
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 86.109, 86.109, 153.825, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 20.2

Other elements in 2a9b:

The structure of Crystal Structure of R138Q Mutant of Recombinant Sulfite Oxidase at Resting State also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Crystal Structure of R138Q Mutant of Recombinant Sulfite Oxidase at Resting State (pdb code 2a9b). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total only one binding site of Molybdenum was determined in the Crystal Structure of R138Q Mutant of Recombinant Sulfite Oxidase at Resting State, PDB code: 2a9b:

Molybdenum binding site 1 out of 1 in 2a9b

Go back to Molybdenum Binding Sites List in 2a9b
Molybdenum binding site 1 out of 1 in the Crystal Structure of R138Q Mutant of Recombinant Sulfite Oxidase at Resting State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Crystal Structure of R138Q Mutant of Recombinant Sulfite Oxidase at Resting State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo1501

b:34.1
occ:1.00
O A:HOH2501 1.6 26.6 1.0
O A:HOH2502 2.2 30.7 1.0
S1' A:MTE501 2.3 30.1 1.0
S2' A:MTE501 2.4 30.2 1.0
SG A:CYS185 2.5 32.8 1.0
C1' A:MTE501 3.3 31.0 1.0
C2' A:MTE501 3.3 31.7 1.0
OE1 A:GLN138 3.4 42.1 1.0
CB A:CYS185 3.5 32.2 1.0
CA A:CYS185 3.8 32.1 1.0
N A:ALA186 3.8 32.8 1.0
N A:ALA297 3.9 30.9 1.0
OH A:TYR322 4.0 41.4 1.0
CD A:GLN138 4.1 40.8 1.0
CE1 A:TYR322 4.2 42.4 1.0
C A:CYS185 4.3 32.5 1.0
CZ A:TYR322 4.3 41.1 1.0
CA A:ALA297 4.4 31.4 1.0
CB A:ALA297 4.5 31.3 1.0
C A:GLY296 4.6 30.3 1.0
CG A:GLN138 4.7 37.4 1.0
C6 A:MTE501 4.7 31.4 1.0
C3' A:MTE501 4.8 32.3 1.0
CA A:GLY296 4.8 29.9 1.0
CL A:CL502 4.8 61.8 1.0
CB A:ALA186 4.9 32.9 1.0
CA A:ALA186 4.9 33.5 1.0
CB A:GLN138 4.9 34.8 1.0

Reference:

E.Karakas, H.L.Wilson, T.N.Graf, S.Xiang, S.Jaramillo-Busquets, K.V.Rajagopalan, C.Kisker. Structural Insights Into Sulfite Oxidase Deficiency J.Biol.Chem. V. 280 33506 2005.
ISSN: ISSN 0021-9258
PubMed: 16048997
DOI: 10.1074/JBC.M505035200
Page generated: Tue Dec 15 05:16:51 2020

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