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4AWD

Crystal structure of the beta-porphyranase BpGH16B (BACPLE_01689) from the human gut bacterium Bacteroides plebeius

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033916molecular_functionbeta-agarase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0033916molecular_functionbeta-agarase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1321
ChainResidue
AGLU54
AASN56
AGLY91
AASP309
AHOH2038

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1322
ChainResidue
AASP175
AGLU284
AARG76
ATHR147
ATRP149
AGLU173

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1321
ChainResidue
BGLU54
BASN56
BGLY91
BASP309
BHOH2024
BHOH2027

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1322
ChainResidue
BTRP149
BGLU173
BASP175
BGLU178
BHIS205
BGLU284
BHOH2089

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:G0L322
ChainResidueDetails
AGLU173
BGLU173

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:G0L322
ChainResidueDetails
AGLU178
BGLU178

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:D7GXG0
ChainResidueDetails
ATRP72
BGLU284
AARG76
AGLU173
AGLU178
AGLU284
BTRP72
BARG76
BGLU173
BGLU178

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PDB entries from 2024-07-24

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