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3A24

Crystal structure of BT1871 retaining glycosidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004557molecular_functionalpha-galactosidase activity
A0008152biological_processmetabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004557molecular_functionalpha-galactosidase activity
B0008152biological_processmetabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MES A 1267
ChainResidue
AARG586
AGLY588
AASP589
BARG98

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1268
ChainResidue
AHOH1131
AHOH1132
AGLU174
AGLU464
AGLU470
AHOH1129
AHOH1130

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 1269
ChainResidue
BGLU174
BGLU464
BGLU470
BHOH1173
BHOH1174
BHOH1175
BHOH1176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:19646996
ChainResidueDetails
AASP415
BASP415

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:19646996
ChainResidueDetails
AGLU470
BGLU470

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19646996
ChainResidueDetails
AGLU174
AGLU464
AGLU470
BGLU174
BGLU464
BGLU470

218853

PDB entries from 2024-04-24

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