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1W9P

Specificity and affinity of natural product cyclopentapeptide inhibitors against Aspergillus fumigatus, human and bacterial chitinaseFra

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008061molecular_functionchitin binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008061molecular_functionchitin binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A1433
ChainResidue
AHIS229
ALEU230
ALYS231
AASP232
AHOH2437
AHOH2706
AHOH2708

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A1434
ChainResidue
AHOH2709
AHOH2710
AASN181
AASP182

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1435
ChainResidue
ATHR149
AASP150
AHOH2713
AHOH2714
AHOH2715

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A1436
ChainResidue
AHOH2169
AHOH2717
AHOH2718
AHOH2719
AHOH2720
BARG283
BALA289
BHOH2445

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1432
ChainResidue
BTHR149
BASP150
BHOH2644
BHOH2645

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B1433
ChainResidue
BHIS229
BLEU230
BLYS231
BASP232
BHOH2373
BHOH2646

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1434
ChainResidue
BASN181
BASP182
BHOH2647
BHOH2648

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGLDIDwE
ChainResidueDetails
APHE169-GLU177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues728
DetailsDomain: {"description":"GH18","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16183021","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A3B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP175
ATYR245
AGLU177

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
BASP175
BTYR245
BGLU177

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP175
AGLU177

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
BASP175
BGLU177

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AGLU177
AASP173

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
BGLU177
BASP173

243083

PDB entries from 2025-10-15

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