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2IW0

Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A1255
ChainResidue
AASP50
AHIS104
AHIS108
AACT1256
AHOH2173

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ACT A1256
ChainResidue
APRO144
ATYR145
AHIS206
AHIS254
AZN1255
AHOH2173
AASP49
AASP50
AHIS104
AHIS108

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A1257
ChainResidue
AASP110
AASN112
AARG132
AILE133
ASER147
AHOH2085

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A1258
ChainResidue
AARG93
AGLU210
AHOH2174

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A1259
ChainResidue
AARG124
AHIS254
AHOH2132

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A1260
ChainResidue
AARG124
AARG131
ALYS247
AHIS249
AHIS250
AHIS251
AHIS254
AHOH2175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:16878976
ChainResidueDetails
AASP49

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:16878976
ChainResidueDetails
AHIS206

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16878976, ECO:0007744|PDB:2IW0
ChainResidueDetails
AASP49
ATYR145

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:16878976, ECO:0007744|PDB:2IW0
ChainResidueDetails
AASP50
AHIS104
AHIS108

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Prevents de-N-acetylated sugar residues from interacting with the active site => ECO:0000303|PubMed:16878976
ChainResidueDetails
ALYS171

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PDB entries from 2024-10-16

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