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1O4Z

THE THREE-DIMENSIONAL STRUCTURE OF BETA-AGARASE B FROM ZOBELLIA GALACTANIVORANS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0009279cellular_componentcell outer membrane
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033916molecular_functionbeta-agarase activity
A0042803molecular_functionprotein homodimerization activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0009279cellular_componentcell outer membrane
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0033916molecular_functionbeta-agarase activity
B0042803molecular_functionprotein homodimerization activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0009279cellular_componentcell outer membrane
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0033916molecular_functionbeta-agarase activity
C0042803molecular_functionprotein homodimerization activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0009279cellular_componentcell outer membrane
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0033916molecular_functionbeta-agarase activity
D0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 1001
ChainResidue
BVAL239

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 1002
ChainResidue
CGLU197
CSER198

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA D 1003
ChainResidue
DASN83
DGLU85
DGLY127
DASP343

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1004
ChainResidue
AGLY127
AASP343
AHOH2119
AASN83
AGLU85

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 1005
ChainResidue
BASN83
BGLU85
BGLY127
BASP343

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA C 1006
ChainResidue
CASN83
CGLY127
CASP343
CHOH2198

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 1007
ChainResidue
AARG246

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA B 1008
ChainResidue
BGLU128
BHOH2232

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA C 1009
ChainResidue
CLYS118
CARG119

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EPE C 2001
ChainResidue
CPRO112
CASP173
CTRP175
CGLU184
CASP186
CGLU189
CGLU308
CGLN310
CTHR311
CTRP312

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EPE A 2002
ChainResidue
APRO112
AASP173
ATRP175
AGLU184
AASP186
AGLU189
AGLU308
AGLN310
ATHR311

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EPE D 2003
ChainResidue
DTRP175
DGLU184
DASP186
DGLU189
DGLU308
DGLN310

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EPE B 2004
ChainResidue
BPRO112
BTRP175
BGLU184
BASP186
BGLU189
BGLU308
BGLN310
BTHR311
BHOH2084

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"G0L322","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"G0L322","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22778272","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues885
DetailsDomain: {"description":"GH16","evidences":[{"source":"PROSITE-ProRule","id":"PRU01098","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 2ayh
ChainResidueDetails
AASP186
AGLU197
AGLU184

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PDB entries from 2025-07-30

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