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6HY3

Three-dimensional structure of AgaC 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 Residues5
Detailsbinding site for residue MG A 401
ChainResidue
AGLU95
AGLY128
AASP318
AHOH520
AHOH630

site_idAC2
Number of Residues10
Detailsbinding site for residue GOL A 402
ChainResidue
AGLU188
AASP190
AGLU193
ATRP291
AHOH563
AHOH609
AHIS63
ATYR112
ATHR175
ATRP177

site_idAC3
Number of Residues9
Detailsbinding site for residue GOL A 403
ChainResidue
AGLU95
AGLN209
AASN228
APHE229
AASP230
AGLU233
AHOH509
AHOH577
AHOH580

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO A 404
ChainResidue
AHIS65
APHE72
AARG224
AALA237
APRO239
AHOH562
AHOH625

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 405
ChainResidue
AMET150
AASN179
AASN285
AHOH501
AHOH541

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:G0L322
ChainResidueDetails
AGLU188

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:G0L322
ChainResidueDetails
AGLU193

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:D7GXG0
ChainResidueDetails
ATRP110
AGLU188
AGLU193

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:G0L322
ChainResidueDetails
ALYS119
ALYS133
AARG224

227344

PDB entries from 2024-11-13

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