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3WVJ

The crystal structure of native glycosidic hydrolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE B3P A 301
ChainResidue
AGLU140
AHOH437
AHOH468
AHOH533
AHOH559
ATYR154
AGLU162
ATRP215
AVAL220
ATRP223
AB3P302
AHOH420
AHOH427

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE B3P A 302
ChainResidue
AASN56
APHE60
AGLU94
APHE123
ATYR125
APRO128
ATRP134
AGLU136
AASN213
AB3P301
AHOH410
AHOH413
AHOH420
AHOH490
AHOH554
BASP53

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE B3P B 301
ChainResidue
BGLU136
BGLU140
BTYR154
BGLU162
BTRP223
BB3P302
BHOH437
BHOH463
BHOH465
BHOH546

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE B3P B 302
ChainResidue
AASP53
BASN56
BPHE60
BGLU94
BARG96
BPHE123
BTYR125
BTRP134
BGLU136
BASN213
BB3P301
BHOH415
BHOH437
BHOH465
BHOH571

Functional Information from PROSITE/UniProt
site_idPS01034
Number of Residues11
DetailsGH16_1 Glycosyl hydrolases family 16 active sites. EIDI.EflGKdT
ChainResidueDetails
AGLU136-THR146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10064
ChainResidueDetails
AGLU136
BGLU136

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10064
ChainResidueDetails
AGLU140
BGLU140

218853

PDB entries from 2024-04-24

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