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1HM2

ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016829molecular_functionlyase activity
A0030246molecular_functioncarbohydrate binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE:
ChainResidueDetails
AHIS225
ATYR234
AARG288

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLU405
AASP407
AASP416
ATYR417

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: O-linked (Man...) serine
ChainResidueDetails
ASER328
ASER455

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c82
ChainResidueDetails
AASN175
ATYR234
AHIS225

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c82
ChainResidueDetails
ATYR234
AHIS225
AARG288

site_idMCSA1
Number of Residues5
DetailsM-CSA 441
ChainResidueDetails
AASN175electrostatic stabiliser
AHIS225electrostatic stabiliser, modifies pKa
ATYR234proton shuttle (general acid/base)
AARG288electrostatic stabiliser, modifies pKa
AGLU371modifies pKa

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PDB entries from 2024-07-24

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