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Cobalt in PDB 1ccw: Structure of the Coenzyme B12 Dependent Enzyme Glutamate Mutase From Clostridium Cochlearium

Enzymatic activity of Structure of the Coenzyme B12 Dependent Enzyme Glutamate Mutase From Clostridium Cochlearium

All present enzymatic activity of Structure of the Coenzyme B12 Dependent Enzyme Glutamate Mutase From Clostridium Cochlearium:
5.4.99.1;

Protein crystallography data

The structure of Structure of the Coenzyme B12 Dependent Enzyme Glutamate Mutase From Clostridium Cochlearium, PDB code: 1ccw was solved by R.Reitzer, K.Gruber, C.Kratky, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 64.430, 113.050, 108.300, 90.00, 95.79, 90.00
R / Rfree (%) 13.7 / 17.3

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structure of the Coenzyme B12 Dependent Enzyme Glutamate Mutase From Clostridium Cochlearium (pdb code 1ccw). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Structure of the Coenzyme B12 Dependent Enzyme Glutamate Mutase From Clostridium Cochlearium, PDB code: 1ccw:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 1ccw

Go back to Cobalt Binding Sites List in 1ccw
Cobalt binding site 1 out of 2 in the Structure of the Coenzyme B12 Dependent Enzyme Glutamate Mutase From Clostridium Cochlearium


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of the Coenzyme B12 Dependent Enzyme Glutamate Mutase From Clostridium Cochlearium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co800

b:9.2
occ:1.00
CO A:CNC800 0.0 9.2 1.0
N24 A:CNC800 1.9 8.1 1.0
N21 A:CNC800 1.9 9.2 1.0
N23 A:CNC800 1.9 9.5 1.0
N22 A:CNC800 1.9 7.6 1.0
C1A A:CNC800 1.9 23.7 1.0
NE2 A:HIS16 2.3 11.9 1.0
C19 A:CNC800 2.8 8.1 1.0
C9 A:CNC800 2.9 7.3 1.0
C1 A:CNC800 2.9 9.3 1.0
C11 A:CNC800 2.9 8.5 1.0
C4 A:CNC800 2.9 9.7 1.0
C16 A:CNC800 2.9 6.4 1.0
C14 A:CNC800 2.9 6.4 1.0
C6 A:CNC800 3.0 8.2 1.0
N1A A:CNC800 3.1 27.0 1.0
CE1 A:HIS16 3.2 9.8 1.0
C10 A:CNC800 3.2 8.1 1.0
CD2 A:HIS16 3.4 10.1 1.0
C5 A:CNC800 3.4 7.7 1.0
C15 A:CNC800 3.4 7.3 1.0
C20 A:CNC800 3.6 8.9 1.0
C18 A:CNC800 4.1 7.4 1.0
C2 A:CNC800 4.1 7.1 1.0
C17 A:CNC800 4.2 7.0 1.0
C3 A:CNC800 4.2 8.1 1.0
C12 A:CNC800 4.2 6.6 1.0
C8 A:CNC800 4.2 9.1 1.0
C13 A:CNC800 4.2 8.7 1.0
C7 A:CNC800 4.2 9.4 1.0
ND1 A:HIS16 4.4 11.0 1.0
O A:HOH844 4.4 29.1 1.0
CG A:HIS16 4.5 10.7 1.0
C26 A:CNC800 4.5 7.6 1.0
C37 A:CNC800 4.7 8.4 1.0
O39 A:CNC800 4.7 16.4 1.0
O B:HOH940 4.8 10.8 1.0
C48 A:CNC800 4.8 7.3 1.0
C46 A:CNC800 4.8 8.5 1.0
C54 A:CNC800 4.9 8.1 1.0
C35 A:CNC800 4.9 8.1 1.0
C53 A:CNC800 4.9 6.8 1.0
C41 A:CNC800 4.9 7.0 1.0

Cobalt binding site 2 out of 2 in 1ccw

Go back to Cobalt Binding Sites List in 1ccw
Cobalt binding site 2 out of 2 in the Structure of the Coenzyme B12 Dependent Enzyme Glutamate Mutase From Clostridium Cochlearium


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Structure of the Coenzyme B12 Dependent Enzyme Glutamate Mutase From Clostridium Cochlearium within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Co800

b:10.4
occ:1.00
CO C:CNC800 0.0 10.4 1.0
N21 C:CNC800 1.9 10.3 1.0
N24 C:CNC800 1.9 9.2 1.0
N23 C:CNC800 1.9 8.0 1.0
N22 C:CNC800 1.9 7.8 1.0
C1A C:CNC800 1.9 30.8 1.0
NE2 C:HIS16 2.3 11.3 1.0
C19 C:CNC800 2.8 8.3 1.0
C11 C:CNC800 2.9 7.9 1.0
C9 C:CNC800 2.9 8.2 1.0
C1 C:CNC800 2.9 9.3 1.0
C4 C:CNC800 2.9 9.3 1.0
C16 C:CNC800 2.9 8.1 1.0
C14 C:CNC800 2.9 7.6 1.0
C6 C:CNC800 3.0 9.5 1.0
N1A C:CNC800 3.1 25.6 1.0
CE1 C:HIS16 3.2 12.9 1.0
C10 C:CNC800 3.2 7.6 1.0
CD2 C:HIS16 3.3 9.6 1.0
C5 C:CNC800 3.4 9.8 1.0
C15 C:CNC800 3.4 7.0 1.0
C20 C:CNC800 3.6 9.7 1.0
C18 C:CNC800 4.1 7.4 1.0
C2 C:CNC800 4.1 7.4 1.0
C12 C:CNC800 4.2 8.4 1.0
C3 C:CNC800 4.2 8.8 1.0
C8 C:CNC800 4.2 10.1 1.0
C13 C:CNC800 4.2 7.6 1.0
C17 C:CNC800 4.2 7.3 1.0
C7 C:CNC800 4.2 8.9 1.0
ND1 C:HIS16 4.3 10.7 1.0
CG C:HIS16 4.4 10.1 1.0
O C:HOH849 4.5 28.5 1.0
C26 C:CNC800 4.5 10.2 1.0
C37 C:CNC800 4.7 8.6 1.0
O39 C:CNC800 4.7 17.2 1.0
O D:HOH912 4.8 12.8 1.0
C48 C:CNC800 4.8 7.0 1.0
C46 C:CNC800 4.8 8.1 1.0
C53 C:CNC800 4.9 7.6 1.0
C35 C:CNC800 4.9 9.6 1.0
C54 C:CNC800 4.9 10.2 1.0
C41 C:CNC800 4.9 8.8 1.0

Reference:

R.Reitzer, K.Gruber, G.Jogl, U.G.Wagner, H.Bothe, W.Buckel, C.Kratky. Glutamate Mutase From Clostridium Cochlearium: the Structure of A Coenzyme B12-Dependent Enzyme Provides New Mechanistic Insights Structure Fold.Des. V. 7 891 1999.
ISSN: ISSN 0969-2126
PubMed: 10467146
DOI: 10.1016/S0969-2126(99)80116-6
Page generated: Sun Dec 13 10:34:24 2020

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