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1VD5

Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0052757molecular_functionchondroitin hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GLY A 401
ChainResidue
ATRP42
AASP149
AGLN211
ATRP219
AARG221
ATRP225
ATYR338
ADTT501
AHOH1443

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GLY A 402
ChainResidue
AGLY320
AARG334
AARG335
AHOH1193
AHOH1237
AHOH1325

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GLY A 403
ChainResidue
AASP60
AGLN62
ATYR63
AHOH1312

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GLY A 404
ChainResidue
ALEU290

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DTT A 501
ChainResidue
ATRP134
AHIS210
AGLN211
ATYR338
AGLY401
ADTT502
AHOH1020
AHOH1031

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DTT A 502
ChainResidue
ATRP134
AHIS210
ADTT501
AHOH1451

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 601
ChainResidue
ATYR55
AGLY59
AHOH1247

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:21147778
ChainResidueDetails
AASP88

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:21147778
ChainResidueDetails
AASP149

221716

PDB entries from 2024-06-26

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