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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 Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:12970344
ChainResidueDetails
AGLU147

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:12970344
ChainResidueDetails
AGLU152

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15062085
ChainResidueDetails
ATRP73
AASN82
AGLN96
AGLU144
AARG176
AASP271

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

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PDB entries from 2024-10-09

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