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Cobalt in PDB 2c79: The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion.

Enzymatic activity of The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion.

All present enzymatic activity of The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion.:
3.1.1.72;

Protein crystallography data

The structure of The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion., PDB code: 2c79 was solved by E.J.Taylor, P.J.Turkenburg, F.Vincent, A.M.Brzozowski, T.M.Gloster, C.Dupont, F.Shareck, M.S.J.Centeno, J.A.M.Prates, L.M.A.Ferreira, C.M.G.A.Fontes, P.Biely, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 74.74 / 1.5
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 105.775, 105.775, 35.349, 90.00, 90.00, 90.00
R / Rfree (%) 13 / 17.2

Cobalt Binding Sites:

The binding sites of Cobalt atom in the The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion. (pdb code 2c79). 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 The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion., PDB code: 2c79:

Cobalt binding site 1 out of 1 in 2c79

Go back to Cobalt Binding Sites List in 2c79
Cobalt binding site 1 out of 1 in the The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion.


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co1685

b:7.2
occ:1.00
 O A:HOH2334 2.1 9.8 1.0
O A:HOH2333 2.1 9.1 1.0
O A:HOH2332 2.1 10.0 1.0
NE2 A:HIS539 2.2 6.1 1.0
O A:HOH2335 2.2 10.2 1.0
OD1 A:ASP488 2.3 6.3 1.0
CD2 A:HIS539 3.1 7.3 1.0
CE1 A:HIS539 3.2 6.2 1.0
CG A:ASP488 3.3 6.7 1.0
OD2 A:ASP488 3.7 8.9 1.0
O A:HOH2029 4.0 13.2 1.0
O A:HOH2094 4.0 9.0 1.0
CB A:ASP487 4.1 5.9 1.0
O A:HOH2150 4.2 17.9 1.0
OD2 A:ASP487 4.2 8.9 1.0
O A:HOH2152 4.2 15.2 1.0
ND1 A:HIS539 4.3 6.7 1.0
CG A:HIS539 4.3 5.9 1.0
NE2 A:HIS630 4.4 9.3 1.0
O A:HOH2208 4.5 21.4 1.0
CD2 A:HIS630 4.5 7.2 1.0
CG A:ASP487 4.6 8.2 1.0
CB A:ASP488 4.7 5.5 1.0
CD1 A:TYR543 4.9 8.3 1.0
CA A:ASP488 5.0 5.5 1.0

Reference:

E.J.Taylor, T.M.Gloster, P.J.Turkenburg, F.Vincent, A.M.Brzozowski, C.Dupont, F.Shareck, M.S.J.Centeno, J.A.M.Prates, V.Puchart, L.M.A.Ferreira, C.M.G.A.Fontes, P.Biely, G.J.Davies. Structure and Activity of Two Metal-Ion Dependent Acetyl Xylan Esterases Involved in Plant Cell Wall Degradation Reveals A Close Similarity to Peptidoglycan Deacetylases. J.Biol.Chem. V. 281 10968 2006.
ISSN: ISSN 0021-9258
PubMed: 16431911
DOI: 10.1074/JBC.M513066200
Page generated: Sun Jul 13 18:04:41 2025

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