Atomistry » Zinc » PDB 3wod-3wyl » 3wrg
Atomistry »
  Zinc »
    PDB 3wod-3wyl »
      3wrg »

Zinc in PDB 3wrg: The Complex Structure of HYPBA1 with L-Arabinose

Enzymatic activity of The Complex Structure of HYPBA1 with L-Arabinose

All present enzymatic activity of The Complex Structure of HYPBA1 with L-Arabinose:
3.2.1.185;

Protein crystallography data

The structure of The Complex Structure of HYPBA1 with L-Arabinose, PDB code: 3wrg 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 / 2.23
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.586, 77.586, 254.176, 90.00, 90.00, 120.00
R / Rfree (%) 20.4 / 24.4

Zinc Binding Sites:

The binding sites of Zinc atom in the The Complex Structure of HYPBA1 with L-Arabinose (pdb code 3wrg). 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 Complex Structure of HYPBA1 with L-Arabinose, PDB code: 3wrg:

Zinc binding site 1 out of 1 in 3wrg

Go back to Zinc Binding Sites List in 3wrg
Zinc binding site 1 out of 1 in the The Complex Structure of HYPBA1 with L-Arabinose


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Complex Structure of HYPBA1 with L-Arabinose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn702

b:44.2
occ:1.00
OE2 A:GLU338 2.2 37.2 1.0
SG A:CYS418 2.3 39.6 1.0
SG A:CYS340 2.3 43.9 1.0
SG A:CYS417 2.4 45.7 1.0
N A:CYS418 3.1 42.2 1.0
CB A:CYS340 3.2 36.5 1.0
CD A:GLU338 3.2 41.8 1.0
CB A:CYS417 3.3 44.6 1.0
CB A:CYS418 3.4 44.2 1.0
CA A:CYS418 3.5 42.2 1.0
C A:CYS417 3.6 43.9 1.0
CG A:GLU338 3.6 39.7 1.0
CA A:CYS417 4.0 44.2 1.0
N A:CYS340 4.0 35.7 1.0
CA A:CYS340 4.2 36.3 1.0
O A:CYS417 4.2 44.8 1.0
C2' A:FUB701 4.3 44.2 1.0
OE1 A:GLU338 4.4 44.9 1.0
CZ A:TYR386 4.4 42.8 1.0
CE1 A:TYR386 4.4 40.2 1.0
N A:CYS417 4.5 45.3 1.0
CE2 A:TYR386 4.6 42.8 1.0
CD1 A:TYR386 4.7 41.7 1.0
O2' A:FUB701 4.7 42.0 1.0
CD2 A:TYR386 4.8 43.6 1.0
OH A:TYR386 4.8 41.6 1.0
CG A:TYR386 4.9 43.7 1.0
C1' A:FUB701 5.0 44.9 1.0
C A:CYS418 5.0 44.8 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 04:57:56 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy