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4ASM

Crystal structure of the catalytic domain of beta-agarase D from Zobellia galactanivorans

Functional Information from GO Data
ChainGOidnamespacecontents
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0033916molecular_functionbeta-agarase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1359
ChainResidue
BASP4
BASP29
BASN31
BGLY84
BASP349
BHOH2017

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IMD B 1360
ChainResidue
BASP157
BGLU160
BGLU321
BGLN323
BASP144
BTRP146
BGLU155

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PEG B 1361
ChainResidue
BGLU160
BTYR162
BHIS179
BGLN195
BTRP202
BGLN323
BTRP325
BHOH2365
BHOH2556
BHOH2594
BHOH2595

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"G0L322","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"G0L322","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"G0L322","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"D7GXG0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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