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Cobalt in PDB 7wuz: Structural Study of the Complex of Cblc Methylmalonic Aciduria and Homocysteinuria-Related Protein Mmachc with Cyanocobalamin

Enzymatic activity of Structural Study of the Complex of Cblc Methylmalonic Aciduria and Homocysteinuria-Related Protein Mmachc with Cyanocobalamin

All present enzymatic activity of Structural Study of the Complex of Cblc Methylmalonic Aciduria and Homocysteinuria-Related Protein Mmachc with Cyanocobalamin:
1.16.1.6; 2.5.1.151;

Protein crystallography data

The structure of Structural Study of the Complex of Cblc Methylmalonic Aciduria and Homocysteinuria-Related Protein Mmachc with Cyanocobalamin, PDB code: 7wuz was solved by Y.Feng, X.Qin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.37 / 1.93
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 72.968, 96.327, 47.257, 90, 111.06, 90
R / Rfree (%) 16.5 / 20.7

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structural Study of the Complex of Cblc Methylmalonic Aciduria and Homocysteinuria-Related Protein Mmachc with Cyanocobalamin (pdb code 7wuz). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Structural Study of the Complex of Cblc Methylmalonic Aciduria and Homocysteinuria-Related Protein Mmachc with Cyanocobalamin, PDB code: 7wuz:

Cobalt binding site 1 out of 1 in 7wuz

Go back to Cobalt Binding Sites List in 7wuz
Cobalt binding site 1 out of 1 in the Structural Study of the Complex of Cblc Methylmalonic Aciduria and Homocysteinuria-Related Protein Mmachc with Cyanocobalamin


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structural Study of the Complex of Cblc Methylmalonic Aciduria and Homocysteinuria-Related Protein Mmachc with Cyanocobalamin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co301

b:19.9
occ:1.00
CO A:CNC301 0.0 19.9 1.0
C1A A:CNC301 1.8 32.3 1.0
N24 A:CNC301 1.8 18.9 1.0
N21 A:CNC301 1.8 22.5 1.0
N23 A:CNC301 1.9 28.9 1.0
N22 A:CNC301 1.9 27.2 1.0
C19 A:CNC301 2.7 21.2 1.0
C9 A:CNC301 2.8 35.4 1.0
C1 A:CNC301 2.8 15.8 1.0
C14 A:CNC301 2.8 25.7 1.0
C11 A:CNC301 2.8 31.7 1.0
C4 A:CNC301 2.8 16.9 1.0
C16 A:CNC301 2.9 18.7 1.0
N1A A:CNC301 2.9 39.6 1.0
C6 A:CNC301 2.9 24.8 1.0
C10 A:CNC301 3.2 31.1 1.0
C15 A:CNC301 3.3 27.0 1.0
C5 A:CNC301 3.3 21.4 1.0
C20 A:CNC301 3.4 16.3 1.0
C2 A:CNC301 4.1 14.2 1.0
C18 A:CNC301 4.1 16.2 1.0
C13 A:CNC301 4.1 27.4 1.0
C3 A:CNC301 4.1 12.4 1.0
C8 A:CNC301 4.1 34.4 1.0
O44 A:CNC301 4.2 38.2 1.0
C7 A:CNC301 4.2 30.6 1.0
C17 A:CNC301 4.2 19.5 1.0
C12 A:CNC301 4.2 35.0 1.0
C26 A:CNC301 4.5 12.7 1.0
O39 A:CNC301 4.6 35.6 1.0
C49 A:CNC301 4.6 43.6 1.0
C37 A:CNC301 4.7 37.8 1.0
C41 A:CNC301 4.7 25.9 1.0
C35 A:CNC301 4.8 19.9 1.0
C53 A:CNC301 4.8 21.6 1.0
C46 A:CNC301 4.9 33.2 1.0
C48 A:CNC301 4.9 31.1 1.0
O4 A:TLA302 5.0 35.2 1.0
C54 A:CNC301 5.0 20.2 1.0

Reference:

Y.Feng, X.Qin. Structural Study of the Complex of Cblc Methylmalonic Aciduria and Homocysteinuria-Related Protein Mmachc with Cyanocobalamin To Be Published.
Page generated: Tue Apr 4 23:04:53 2023

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