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3ARQ

Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - complex structure with IDARUBICIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004568molecular_functionchitinase activity
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0008061molecular_functionchitin binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE DM5 A 606
ChainResidue
ATRP275
AHOH813
AHOH1009
AHOH1090
AHOH1097
AHOH1229
AHOH1290
AGOL3500
AGLY320
AGLY321
ALYS370
AASP392
APHE393
ATRP397
ATYR435
AHOH805

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL A 3500
ChainResidue
APHE316
AGLY365
AVAL366
AGLY367
ALYS370
AMET389
ATYR391
AASP392
ATYR435
ADM5606
AHOH805
AHOH813

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 3501
ChainResidue
AGLU114
ACYS121
ASER122
ALYS123
AGLY206
AGLY207
AASN211
AHOH868
AHOH997
AHOH1147

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 3502
ChainResidue
ALYS151
AHIS549
AASP578
AASN581
AALA582
AGLU585
AHOH1215
AHOH1266
AHOH1300

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. YDGVDIDwE
ChainResidueDetails
ATYR307-GLU315

246704

PDB entries from 2025-12-24

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