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2YBT

Crystal structure of human acidic chitinase in complex with bisdionin C

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
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0008061molecular_functionchitin binding
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0008061molecular_functionchitin binding
E0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
E0005975biological_processcarbohydrate metabolic process
E0008061molecular_functionchitin binding
F0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
F0005975biological_processcarbohydrate metabolic process
F0008061molecular_functionchitin binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1398
ChainResidue
ATRP31
AARG35
AGLU297
ATRP360
ADW01399
AHOH2190
AHOH2201

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1398
ChainResidue
BGLU297
BTRP360
BDW01399
BHOH2185
BTRP31
BARG35

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL C 1398
ChainResidue
CTRP31
CARG35
CGLU297
CTRP360
CDW01399
CHOH2006
CHOH2194

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 1398
ChainResidue
DTRP31
DARG35
DGLU297
DTRP360
DDW01399
DHOH2145

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL E 1398
ChainResidue
ETRP31
EARG35
ETRP360
EDW01399
EHOH2128
EHOH2186

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL F 1398
ChainResidue
FTRP31
FARG35
FGLU297
FILE300
FTRP360
FDW01399
FHOH2118

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DW0 A 1399
ChainResidue
ATRP31
APHE58
AGLY98
ATRP99
AASN100
AASP138
AGLU140
AMET210
ATYR212
ATYR267
ATRP360
AGOL1398
AHOH2052
AHOH2119

site_idAC8
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DW0 B 1399
ChainResidue
BTRP31
BPHE58
BGLY98
BTRP99
BASN100
BASP138
BGLU140
BMET210
BTYR212
BTYR267
BTRP360
BGOL1398
BHOH2193

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DW0 C 1399
ChainResidue
CTRP31
CPHE58
CGLY98
CTRP99
CASN100
CASP138
CGLU140
CMET210
CTYR212
CTYR267
CTRP360
CGOL1398
CHOH2040
CHOH2195

site_idBC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DW0 D 1399
ChainResidue
DTRP31
DPHE58
DGLY98
DTRP99
DASN100
DASP138
DGLU140
DMET210
DTYR212
DTYR267
DTRP360
DGOL1398
DHOH2037
DHOH2146

site_idBC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DW0 E 1399
ChainResidue
EASP138
EGLU140
EMET210
ETYR212
ETYR267
EGLU297
ETRP360
EGOL1398
EHOH2080
ETRP31
EPHE58
EGLY98
ETRP99
EASN100

site_idBC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DW0 F 1399
ChainResidue
FTRP31
FPHE58
FGLY98
FTRP99
FASN100
FASP138
FGLU140
FMET210
FTYR212
FTYR267
FTRP360
FGOL1398
FHOH2132

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DW0 A 1400
ChainResidue
ATRP99
ATRP218
AHOH2202
DGLN62

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DW0 B 1400
ChainResidue
BTRP99
BTRP218
FGLN62

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DW0 C 1400
ChainResidue
CTRP99
CASP213
CTRP218
CHOH2196
CHOH2197

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DW0 D 1400
ChainResidue
AGLN62
DTRP99
DTRP218

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DW0 E 1400
ChainResidue
ETRP99
ETRP218
EHOH2187

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DW0 F 1400
ChainResidue
BGLN62
FTRP99
FTRP218

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGLDFDwE
ChainResidueDetails
APHE132-GLU140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2208
DetailsDomain: {"description":"GH18","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues54
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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