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Zinc in PDB 3wre: The Crystal Structure of Native HYPBA1 From Bifidobacterium Longum Jcm 1217

Enzymatic activity of The Crystal Structure of Native HYPBA1 From Bifidobacterium Longum Jcm 1217

All present enzymatic activity of The Crystal Structure of Native HYPBA1 From Bifidobacterium Longum Jcm 1217:
3.2.1.185;

Protein crystallography data

The structure of The Crystal Structure of Native HYPBA1 From Bifidobacterium Longum Jcm 1217, PDB code: 3wre was solved by C.H.Huang, Z.Zhu, Y.S.Cheng, H.C.Chan, T.P.Ko, C.C.Chen, I.Wang, M.R.Ho, S.T.Hsu, Y.F.Zeng, Y.N.Huang, J.R.Liu, R.T.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.78
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 75.927, 75.927, 254.031, 90.00, 90.00, 120.00
R / Rfree (%) 22.3 / 27.2

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of Native HYPBA1 From Bifidobacterium Longum Jcm 1217 (pdb code 3wre). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The Crystal Structure of Native HYPBA1 From Bifidobacterium Longum Jcm 1217, PDB code: 3wre:

Zinc binding site 1 out of 1 in 3wre

Go back to Zinc Binding Sites List in 3wre
Zinc binding site 1 out of 1 in the The Crystal Structure of Native HYPBA1 From Bifidobacterium Longum Jcm 1217


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of Native HYPBA1 From Bifidobacterium Longum Jcm 1217 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:78.4
occ:1.00
OE2 A:GLU338 2.5 65.3 1.0
SG A:CYS340 2.5 60.8 1.0
SG A:CYS418 2.5 79.5 1.0
SG A:CYS417 2.7 84.3 1.0
CB A:CYS340 3.0 52.9 1.0
CD A:GLU338 3.2 62.8 1.0
CG A:GLU338 3.3 58.5 1.0
N A:CYS418 3.5 80.7 1.0
CB A:CYS417 3.5 85.0 1.0
CB A:CYS418 3.7 79.4 1.0
CA A:CYS418 3.7 79.3 1.0
N A:CYS340 3.8 49.8 1.0
C A:CYS417 3.8 83.4 1.0
CA A:CYS340 4.0 50.3 1.0
CZ A:TYR386 4.1 80.8 1.0
CE2 A:TYR386 4.2 79.5 1.0
OH A:TYR386 4.2 81.4 1.0
CA A:CYS417 4.3 85.6 1.0
O A:CYS417 4.3 82.7 1.0
OE1 A:GLU338 4.5 64.3 1.0
CE1 A:TYR386 4.5 80.9 1.0
CD2 A:TYR386 4.7 78.2 1.0
CB A:GLU338 4.7 58.4 1.0
N A:THR339 4.9 53.4 1.0
CD1 A:TYR386 4.9 77.9 1.0
C A:THR339 5.0 51.6 1.0

Reference:

C.H.Huang, Z.Zhu, Y.S.Cheng, H.C.Chan, T.P.Ko, C.C.Chen, I.Wang, M.R.Ho, S.T.Hsu, Y.F.Zeng, Y.N.Huang, J.R.Liu, R.T.Guo. Structure and Catalytic Mechanism of A Glycoside Hydrolase Family-127 Beta-L-Arabinofuranosidase (HYPBA1) J Bioprocess Biotech V. 4 00171 2014.
ISSN: ESSN 2155-9821
DOI: 10.4172/2155-9821.1000171
Page generated: Wed Dec 16 04:57:55 2020

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