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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 Residues6
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AGLU140
BGLU140
CGLU140
DGLU140
EGLU140
FGLU140

site_idSWS_FT_FI2
Number of Residues30
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AGLU70
BTRP360
CGLU70
CGLY97
CTYR141
CMET210
CTRP360
DGLU70
DGLY97
DTYR141
DMET210
AGLY97
DTRP360
EGLU70
EGLY97
ETYR141
EMET210
ETRP360
FGLU70
FGLY97
FTYR141
FMET210
ATYR141
FTRP360
AMET210
ATRP360
BGLU70
BGLY97
BTYR141
BMET210

218853

PDB entries from 2024-04-24

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