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Zinc in PDB 2cf5: Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, ATCAD5

Enzymatic activity of Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, ATCAD5

All present enzymatic activity of Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, ATCAD5:
1.1.1.195;

Protein crystallography data

The structure of Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, ATCAD5, PDB code: 2cf5 was solved by B.Youn, R.Camacho, S.Moinuddin, C.Lee, L.B.Davin, N.G.Lewis, C.Kang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10 / 2.0
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 54.220, 54.220, 312.990, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 23.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, ATCAD5 (pdb code 2cf5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, ATCAD5, PDB code: 2cf5:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2cf5

Go back to Zinc Binding Sites List in 2cf5
Zinc binding site 1 out of 2 in the Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, ATCAD5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, ATCAD5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:35.4
occ:1.00
SG A:CYS100 2.5 47.4 1.0
SG A:CYS106 2.5 32.3 1.0
SG A:CYS114 2.5 43.1 1.0
SG A:CYS103 2.7 40.3 1.0
CB A:CYS114 3.1 44.1 1.0
CB A:CYS100 3.4 33.1 1.0
CB A:CYS106 3.5 40.6 1.0
CB A:CYS103 3.6 39.9 1.0
N A:CYS100 3.6 40.4 1.0
N A:GLY101 3.8 40.6 1.0
CA A:CYS100 3.9 38.8 1.0
N A:CYS103 3.9 49.9 1.0
CA A:CYS114 4.0 44.7 1.0
C A:CYS100 4.2 40.0 1.0
N A:CYS106 4.3 41.9 1.0
CA A:CYS103 4.3 45.6 1.0
CD A:PRO115 4.4 39.1 1.0
N A:GLY102 4.4 37.2 1.0
CA A:CYS106 4.5 42.1 1.0
CB A:CYS99 4.6 31.7 1.0
C A:CYS99 4.7 38.0 1.0
CA A:GLY101 4.7 34.8 1.0
O A:CYS103 4.7 46.4 1.0
C A:CYS103 4.8 47.0 1.0
C A:CYS114 4.8 44.0 1.0
SG A:CYS99 4.9 30.9 1.0
N A:PRO115 4.9 40.4 1.0
C A:GLY102 4.9 50.7 1.0
C A:GLY101 5.0 35.0 1.0

Zinc binding site 2 out of 2 in 2cf5

Go back to Zinc Binding Sites List in 2cf5
Zinc binding site 2 out of 2 in the Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, ATCAD5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, ATCAD5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:41.0
occ:1.00
SG A:CYS47 2.4 28.3 1.0
NE2 A:HIS69 2.5 38.3 1.0
SG A:CYS163 2.5 37.9 1.0
OE1 A:GLU70 2.6 24.3 1.0
CB A:CYS47 3.2 22.6 1.0
CE1 A:HIS69 3.2 37.3 1.0
CB A:CYS163 3.2 26.6 1.0
CD2 A:HIS69 3.3 37.0 1.0
CD A:GLU70 3.3 26.3 1.0
CG A:GLU70 3.5 22.4 1.0
ND1 A:HIS69 4.2 33.6 1.0
CG A:HIS69 4.2 33.3 1.0
OE2 A:GLU70 4.3 29.1 1.0
CA A:CYS47 4.4 24.6 1.0
OG1 A:THR49 4.4 32.0 1.0
O A:HOH2053 4.5 40.5 1.0
CA A:CYS163 4.6 26.5 1.0
N A:CYS47 4.7 29.3 1.0
CB A:GLU70 4.9 25.8 1.0
C A:CYS47 5.0 25.9 1.0

Reference:

B.Youn, R.Camacho, S.Moinuddin, C.Lee, L.B.Davin, N.G.Lewis, C.Kang. Crystal Structures and Catalytic Mechanisms of the Arabidopsis Cinnamyl Alcohol Dehydrogenases ATCAD5 and ATCAD4 Org.Biomol.Chem. V. 4 1687 2006.
ISSN: ISSN 1477-0520
PubMed: 16633561
DOI: 10.1039/B601672C
Page generated: Wed Dec 16 03:19:14 2020

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