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1MQR

THE CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE (E386Q) FROM BACILLUS STEAROTHERMOPHILUS T-6

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033939molecular_functionxylan alpha-1,2-glucuronosidase activity
A0045493biological_processxylan catabolic process
A0046559molecular_functionalpha-glucuronidase activity
A2000886biological_processglucuronoxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
ATYR91
AHOH857
AHOH864
ATYR116
AHIS120
AARG123
ASER189
AVAL190
AGLY191
AARG467
ATRP470

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
AARG368
AGLU369
AVAL371
AGLU409
ALEU585
AHOH831
AHOH901
AHOH1123
AHOH1132

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 704
ChainResidue
ASER19
AGLU129
AILE131
AHOH977
AHOH1087
AHOH1236

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 705
ChainResidue
ATYR340
ALYS344
AALA377
AALA565
AGLN566
ATYR567
APHE568
AHOH1115

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 706
ChainResidue
ALYS620
ALYS653
AARG656

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:14573597
ChainResidueDetails
AGLU285

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:14573597
ChainResidueDetails
AASP364
AGLU392

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AGLU158
ALYS281
AARG318
AARG335
ALYS359

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN201
AGLN386
AGLU510
ATRP540

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Participates in a stacking interactions with the sugar rings of 4-O-MeGlcA => ECO:0000250
ChainResidueDetails
ATRP150
ATRP540

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PDB entries from 2024-08-21

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