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3WZ1

Catalytic domain of beta-agarase from Microbulbifer thermotolerans JAMB-A94

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 Residues4
DetailsBINDING SITE FOR RESIDUE NA A 401
ChainResidue
AASP22
AASP46
AGLY90
AASP285

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 402
ChainResidue
AGLU146
ATHR244
AGLY245
ASER247
AHOH560

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
AASN31
APRO32
ALYS36
ATYR210
AASP276
AHOH635
AHOH712

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
AGLU152
ATYR154
AHIS169
AHIS173
AGLN184
AGLN259
ATRP261

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues274
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":"PROSITE-ProRule","id":"PRU01098","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01098","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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