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Zinc in PDB 2cc0: Family 4 Carbohydrate Esterase From Streptomyces Lividans in Complex with Acetate

Enzymatic activity of Family 4 Carbohydrate Esterase From Streptomyces Lividans in Complex with Acetate

All present enzymatic activity of Family 4 Carbohydrate Esterase From Streptomyces Lividans in Complex with Acetate:
3.1.1.72;

Protein crystallography data

The structure of Family 4 Carbohydrate Esterase From Streptomyces Lividans in Complex with Acetate, PDB code: 2cc0 was solved by E.J.Taylor, T.M.Gloster, J.P.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, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 65.65 / 1.6
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 95.538, 47.905, 89.842, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 18.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Family 4 Carbohydrate Esterase From Streptomyces Lividans in Complex with Acetate (pdb code 2cc0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Family 4 Carbohydrate Esterase From Streptomyces Lividans in Complex with Acetate, PDB code: 2cc0:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2cc0

Go back to Zinc Binding Sites List in 2cc0
Zinc binding site 1 out of 2 in the Family 4 Carbohydrate Esterase From Streptomyces Lividans in Complex with Acetate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Family 4 Carbohydrate Esterase From Streptomyces Lividans in Complex with Acetate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn200

b:12.9
occ:0.50
O A:HOH2278 2.1 29.5 1.0
NE2 A:HIS62 2.1 8.6 1.0
OXT A:ACT201 2.2 11.8 0.5
NE2 A:HIS66 2.2 13.7 1.0
O A:ACT201 2.5 11.0 0.5
C A:ACT201 2.7 11.5 0.5
OD1 A:ASP13 2.8 14.0 1.0
CD2 A:HIS66 2.8 13.7 1.0
CD2 A:HIS62 3.1 9.0 1.0
OD2 A:ASP13 3.1 19.1 1.0
CE1 A:HIS62 3.1 9.6 1.0
CG A:ASP13 3.3 14.3 1.0
CE1 A:HIS66 3.4 14.6 1.0
OD2 A:ASP12 3.8 16.0 1.0
CB A:ASP12 4.0 11.1 1.0
O A:HOH2279 4.0 16.4 0.5
CH3 A:ACT201 4.1 12.0 0.5
CG A:HIS66 4.1 11.3 1.0
ND1 A:HIS62 4.2 9.3 1.0
CG A:HIS62 4.2 8.1 1.0
CG A:ASP12 4.3 11.8 1.0
ND1 A:HIS66 4.3 12.8 1.0
NE2 A:HIS155 4.4 11.7 1.0
O A:HOH2233 4.5 14.1 0.5
CD2 A:HIS155 4.6 11.9 1.0
CB A:ASP13 4.7 10.8 1.0
O A:HOH2234 4.7 20.2 0.5
O A:HOH2012 4.7 24.0 1.0
CA A:PRO102 4.8 10.4 1.0
O A:HOH2021 4.8 19.7 1.0

Zinc binding site 2 out of 2 in 2cc0

Go back to Zinc Binding Sites List in 2cc0
Zinc binding site 2 out of 2 in the Family 4 Carbohydrate Esterase From Streptomyces Lividans in Complex with Acetate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Family 4 Carbohydrate Esterase From Streptomyces Lividans in Complex with Acetate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn200

b:14.2
occ:0.50
O B:HOH2284 2.0 32.0 1.0
NE2 B:HIS62 2.1 10.3 1.0
NE2 B:HIS66 2.2 13.9 1.0
OXT B:ACT201 2.4 11.8 0.5
O B:ACT201 2.5 10.4 0.5
C B:ACT201 2.8 11.1 0.5
CD2 B:HIS66 2.8 14.2 1.0
OD1 B:ASP13 2.8 12.5 1.0
CD2 B:HIS62 3.1 8.1 1.0
CE1 B:HIS62 3.1 9.5 1.0
OD2 B:ASP13 3.1 17.8 1.0
CG B:ASP13 3.3 13.4 1.0
CE1 B:HIS66 3.4 14.9 1.0
OD2 B:ASP12 3.8 17.2 1.0
O B:HOH2285 4.0 17.0 0.5
CB B:ASP12 4.0 11.3 1.0
CG B:HIS66 4.1 12.0 1.0
CH3 B:ACT201 4.1 11.4 0.5
ND1 B:HIS62 4.2 9.4 1.0
CG B:HIS62 4.2 7.5 1.0
ND1 B:HIS66 4.3 13.3 1.0
CG B:ASP12 4.4 13.4 1.0
NE2 B:HIS155 4.5 11.4 1.0
O B:HOH2242 4.6 16.3 0.5
O B:HOH2243 4.6 28.4 0.5
CB B:ASP13 4.7 10.1 1.0
CD2 B:HIS155 4.7 10.9 1.0
O B:HOH2017 4.8 15.0 1.0
CA B:PRO102 4.8 11.1 1.0
O B:HOH2009 4.8 27.4 1.0

Reference:

E.J.Taylor, T.M.Gloster, J.P.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: Wed Dec 16 03:19:10 2020

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