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1WVV

Crystal structure of chitinase C mutant E147Q

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004568molecular_functionchitinase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0006952biological_processdefense response
A0016787molecular_functionhydrolase activity
A0016998biological_processcell wall macromolecule catabolic process
A0030246molecular_functioncarbohydrate binding
A0050832biological_processdefense response to fungus
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004568molecular_functionchitinase activity
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0006032biological_processchitin catabolic process
B0006952biological_processdefense response
B0016787molecular_functionhydrolase activity
B0016998biological_processcell wall macromolecule catabolic process
B0030246molecular_functioncarbohydrate binding
B0050832biological_processdefense response to fungus
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 501
ChainResidue
ASER145
AHIS146
BGLN279
BHOH655

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 502
ChainResidue
BILE154
BLYS155
BHOH622

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 503
ChainResidue
BTYR111
BHOH567
BARG105
BTHR110

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 504
ChainResidue
ALYS222
AHOH578

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 505
ChainResidue
AASN275
BHOH518

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 506
ChainResidue
ATYR121
APRO122
AALA123
AHOH603

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 507
ChainResidue
AARG105
ATYR111

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 508
ChainResidue
ALYS155
AASP216
APRO217
AALA218

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 509
ChainResidue
BTHR287
BTHR288

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 510
ChainResidue
BGLN178
BGLY203
BHOH594
BHOH604

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 511
ChainResidue
AGLN178
AGLY203

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 512
ChainResidue
AASN266
BASN266
BGLN269

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 513
ChainResidue
BTYR121
BPRO122
BALA123
BHOH553

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
AGLN147
AILE187
AGLN188
ASER190
AASN194

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 402
ChainResidue
BILE187
BGLN188
BTYR227
BILE256
BHOH583
BHOH596

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 819
ChainResidueDetails
AGLN147promote heterolysis, proton acceptor, proton donor
AGLU156activator, electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor
AASN194steric role

site_idMCSA2
Number of Residues3
DetailsM-CSA 819
ChainResidueDetails
BGLN147promote heterolysis, proton acceptor, proton donor
BGLU156activator, electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor
BASN194steric role

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PDB entries from 2026-02-25

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