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Cobalt in PDB 1qk0: CEL6A with A Non-Hydrolysable Cellotetraose

Enzymatic activity of CEL6A with A Non-Hydrolysable Cellotetraose

All present enzymatic activity of CEL6A with A Non-Hydrolysable Cellotetraose:
3.2.1.91;

Protein crystallography data

The structure of CEL6A with A Non-Hydrolysable Cellotetraose, PDB code: 1qk0 was solved by J.-Y.Zou, T.A.Jones, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.500, 74.690, 91.140, 90.00, 103.19, 90.00
R / Rfree (%) 18.1 / 22.1

Other elements in 1qk0:

The structure of CEL6A with A Non-Hydrolysable Cellotetraose also contains other interesting chemical elements:

Iodine (I) 3 atoms

Cobalt Binding Sites:

The binding sites of Cobalt atom in the CEL6A with A Non-Hydrolysable Cellotetraose (pdb code 1qk0). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the CEL6A with A Non-Hydrolysable Cellotetraose, PDB code: 1qk0:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 1qk0

Go back to Cobalt Binding Sites List in 1qk0
Cobalt binding site 1 out of 2 in the CEL6A with A Non-Hydrolysable Cellotetraose


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of CEL6A with A Non-Hydrolysable Cellotetraose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co900

b:32.9
occ:1.00
OE2 A:GLU146 2.3 19.2 1.0
OE1 A:GLU146 2.4 18.2 1.0
CD A:GLU146 2.7 18.5 1.0
CG A:GLU146 4.1 17.9 1.0
O A:HOH2032 4.4 37.4 1.0
O A:HOH2033 4.7 17.6 1.0

Cobalt binding site 2 out of 2 in 1qk0

Go back to Cobalt Binding Sites List in 1qk0
Cobalt binding site 2 out of 2 in the CEL6A with A Non-Hydrolysable Cellotetraose


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of CEL6A with A Non-Hydrolysable Cellotetraose within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co900

b:43.8
occ:1.00
OE2 B:GLU146 2.6 25.7 1.0
CD B:GLU146 3.5 25.5 1.0
OE1 B:GLU146 4.2 25.4 1.0
CG B:GLU146 4.4 24.4 1.0
CB B:GLU146 4.6 23.2 1.0
OH B:TYR209 4.8 23.8 1.0
CE2 B:TYR209 4.8 23.6 1.0

Reference:

J.-Y.Zou, G.J.Kleywegt, J.Stahlberg, H.Driguez, W.Nerinckx, M.Claeyssens, A.Koivula, T.T.Teeri, T.A.Jones. Crystallographic Evidence For Substrate Ring Distortion and Protein Conformational Changes During Catalysis in Cellobiohydrolase CEL6A From Trichoderma Reesei Structure V. 7 1035 1999.
ISSN: ISSN 0969-2126
PubMed: 10508787
DOI: 10.1016/S0969-2126(99)80171-3
Page generated: Tue Jul 30 14:31:12 2024

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