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Cobalt in PDB 7cel: CBH1 (E217Q) in Complex with Cellohexaose and Cellobiose

Enzymatic activity of CBH1 (E217Q) in Complex with Cellohexaose and Cellobiose

All present enzymatic activity of CBH1 (E217Q) in Complex with Cellohexaose and Cellobiose:
3.2.1.91;

Protein crystallography data

The structure of CBH1 (E217Q) in Complex with Cellohexaose and Cellobiose, PDB code: 7cel was solved by C.Divne, J.Stahlberg, T.A.Jones, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.50 / 1.90
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 83.700, 84.100, 111.500, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 21.5

Cobalt Binding Sites:

The binding sites of Cobalt atom in the CBH1 (E217Q) in Complex with Cellohexaose and Cellobiose (pdb code 7cel). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the CBH1 (E217Q) in Complex with Cellohexaose and Cellobiose, PDB code: 7cel:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 7cel

Go back to Cobalt Binding Sites List in 7cel
Cobalt binding site 1 out of 2 in the CBH1 (E217Q) in Complex with Cellohexaose and Cellobiose


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of CBH1 (E217Q) in Complex with Cellohexaose and Cellobiose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co461

b:52.5
occ:1.00
NE2 A:HIS206 2.5 29.8 1.0
OE1 A:GLU239 2.6 35.6 1.0
OE2 A:GLU239 2.8 35.6 1.0
CD A:GLU239 3.0 35.6 1.0
CE1 A:HIS206 3.2 29.8 1.0
CD2 A:HIS206 3.5 29.8 1.0
ND1 A:HIS206 4.3 29.8 1.0
CG A:GLU239 4.4 35.6 1.0
CG A:HIS206 4.5 29.8 1.0

Cobalt binding site 2 out of 2 in 7cel

Go back to Cobalt Binding Sites List in 7cel
Cobalt binding site 2 out of 2 in the CBH1 (E217Q) in Complex with Cellohexaose and Cellobiose


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of CBH1 (E217Q) in Complex with Cellohexaose and Cellobiose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co1000

b:16.1
occ:0.50
OE2 A:GLU325 2.4 12.9 1.0
OE1 A:GLU295 2.4 17.1 1.0
OE2 A:GLU295 2.5 17.1 1.0
CD A:GLU295 2.8 17.1 1.0
CD A:GLU325 3.3 12.9 1.0
OE1 A:GLU325 3.4 12.9 1.0
ND2 A:ASN301 3.9 15.8 1.0
O A:HOH717 4.0 27.9 1.0
O A:HOH596 4.1 52.0 1.0
CG A:GLU295 4.3 17.1 1.0
CG A:GLU325 4.7 12.9 1.0
CB A:ALA299 4.8 2.0 1.0
OG A:SER297 4.9 12.5 1.0
CG A:ASN301 5.0 15.8 1.0

Reference:

C.Divne, J.Stahlberg, T.T.Teeri, T.A.Jones. High-Resolution Crystal Structures Reveal How A Cellulose Chain Is Bound in the 50 A Long Tunnel of Cellobiohydrolase I From Trichoderma Reesei. J.Mol.Biol. V. 275 309 1998.
ISSN: ISSN 0022-2836
PubMed: 9466911
DOI: 10.1006/JMBI.1997.1437
Page generated: Sun Dec 13 10:55:01 2020

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