Atomistry » Zinc » PDB 7etc-7fa1 » 7exu
Atomistry »
  Zinc »
    PDB 7etc-7fa1 »
      7exu »

Zinc in PDB 7exu: GH127 Beta-L-Arabinofuranosidase HYPBA1 E322Q Mutant Complexed with P- Nitrophenyl Beta-L-Arabinofuranoside

Enzymatic activity of GH127 Beta-L-Arabinofuranosidase HYPBA1 E322Q Mutant Complexed with P- Nitrophenyl Beta-L-Arabinofuranoside

All present enzymatic activity of GH127 Beta-L-Arabinofuranosidase HYPBA1 E322Q Mutant Complexed with P- Nitrophenyl Beta-L-Arabinofuranoside:
3.2.1.185;

Protein crystallography data

The structure of GH127 Beta-L-Arabinofuranosidase HYPBA1 E322Q Mutant Complexed with P- Nitrophenyl Beta-L-Arabinofuranoside, PDB code: 7exu was solved by S.Maruyama, T.Arakawa, C.Yamada, K.Fujita, S.Fushinobu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.31 / 2.30
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 78.182, 78.182, 253.502, 90, 90, 120
R / Rfree (%) 25.2 / 29

Zinc Binding Sites:

The binding sites of Zinc atom in the GH127 Beta-L-Arabinofuranosidase HYPBA1 E322Q Mutant Complexed with P- Nitrophenyl Beta-L-Arabinofuranoside (pdb code 7exu). 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 GH127 Beta-L-Arabinofuranosidase HYPBA1 E322Q Mutant Complexed with P- Nitrophenyl Beta-L-Arabinofuranoside, PDB code: 7exu:

Zinc binding site 1 out of 1 in 7exu

Go back to Zinc Binding Sites List in 7exu
Zinc binding site 1 out of 1 in the GH127 Beta-L-Arabinofuranosidase HYPBA1 E322Q Mutant Complexed with P- Nitrophenyl Beta-L-Arabinofuranoside


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of GH127 Beta-L-Arabinofuranosidase HYPBA1 E322Q Mutant Complexed with P- Nitrophenyl Beta-L-Arabinofuranoside within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:62.3
occ:1.00
 SG A:CYS418 2.0 58.1 1.0
SG A:CYS417 2.0 60.7 1.0
OE2 A:GLU338 2.2 58.2 1.0
SG A:CYS340 2.6 62.4 1.0
CD A:GLU338 3.2 55.0 1.0
CB A:CYS340 3.2 54.2 1.0
N A:CYS418 3.3 69.6 1.0
CB A:CYS417 3.3 71.5 1.0
CB A:CYS418 3.4 59.7 1.0
CG A:GLU338 3.5 55.4 1.0
CA A:CYS418 3.5 62.3 1.0
C A:CYS417 3.6 70.0 1.0
CE1 A:TYR386 3.9 71.4 1.0
CZ A:TYR386 4.0 76.8 1.0
CA A:CYS417 4.0 68.0 1.0
N A:CYS340 4.1 56.5 1.0
C2 A:07Y702 4.2 69.3 1.0
CA A:CYS340 4.2 56.4 1.0
O A:CYS417 4.3 81.4 1.0
CD1 A:TYR386 4.3 77.6 1.0
OH A:TYR386 4.3 74.6 1.0
OE1 A:GLU338 4.3 58.5 1.0
O2 A:07Y702 4.4 62.5 1.0
CE2 A:TYR386 4.5 81.5 1.0
N A:CYS417 4.6 70.5 1.0
C1 A:07Y702 4.7 69.9 1.0
CG A:TYR386 4.7 74.9 1.0
CD2 A:TYR386 4.8 79.6 1.0
CB A:GLU338 4.9 54.8 1.0

Reference:

S.Maruyama, K.Sawano, S.Amaki, T.Suzuki, S.Narita, K.Kimura, T.Arakawa, C.Yamada, Y.Ito, N.Dohmae, K.Fujita, A.Ishiwata, S.Fushinobu. Substrate Complex Structure, Active Site Labeling and Catalytic Role of the Zinc Ion in Cysteine Glycosidase. Glycobiology 2021.
ISSN: ESSN 1460-2423
PubMed: 34735571
DOI: 10.1093/GLYCOB/CWAB103
Page generated: Fri Aug 22 00:06:26 2025

Last articles

Zn in 7ORI
Zn in 7OPL
Zn in 7OPC
Zn in 7OPI
Zn in 7OOP
Zn in 7OOB
Zn in 7OO3
Zn in 7OOD
Zn in 7OOC
Zn in 7ONI
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy