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1HN0

CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006027biological_processglycosaminoglycan catabolic process
A0016829molecular_functionlyase activity
A0030246molecular_functioncarbohydrate binding
A0034000molecular_functionchondroitin-sulfate-ABC endolyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1800
ChainResidue
AHIS43
AMET70
AGLN73
AASP211
AHOH2159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15691229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16108757","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12706721","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HN0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cb8
ChainResidueDetails
ATYR508
AARG560
AHIS501

244349

PDB entries from 2025-11-05

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