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5T9A

Crystal structure of BuGH2Cwt

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue EDO A 902
ChainResidue
AVAL69
ALEU71
APHE73
ALEU84
ALEU802
AASN803
ATYR804

site_idAC2
Number of Residues7
Detailsbinding site for residue EDO A 903
ChainResidue
APRO544
ALYS546
APRO547
AALA548
ATYR568
AALA302
AHIS540

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 904
ChainResidue
AASN309
ALYS311
BPHE243

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 B 901
ChainResidue
BASP103
BLYS184
BTYR216
BSER217

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 C 901
ChainResidue
CASP103
CLYS184
CTYR216
CSER217

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO C 902
ChainResidue
ATYR383
CARG124

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO D 901
ChainResidue
DARG124
DHOH1009

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO D 902
ChainResidue
AGLN469
DPRO464
DTYR466

227111

PDB entries from 2024-11-06

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