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1O4Y

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0033916molecular_functionbeta-agarase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 600
ChainResidue
ATHR161

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 700
ChainResidue
AASP22
ASER47
AASN49
ASER91
AASP279
AHOH902

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 500
ChainResidue
ATYR208
AGLU216
ATYR218
ALYS223
AHOH798
AHOH837
AHOH838
AHOH1017
AASN31
ALYS125

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ATYR50
ATHR51
AGLY90
AARG229
AHOH760
AHOH794
AHOH878
AHOH879
AHOH1050
AHOH1055

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AGLN117
ATYR118
APRO178
APHE179
AASN244
AHOH910

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues268
DetailsDomain: {"description":"GH16","evidences":[{"source":"PROSITE-ProRule","id":"PRU01098","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12970344","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12970344","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15062085","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 2ayh
ChainResidueDetails
AMET151
AASP149
AGLU147

239803

PDB entries from 2025-08-06

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