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1H0G

Complex of a chitinase with the natural product cyclopentapeptide argadin from Clonostachys

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0008061molecular_functionchitin binding
A0030246molecular_functioncarbohydrate binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0008061molecular_functionchitin binding
B0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1500
ChainResidue
ATRP479
AGLY480
AHOH2305
AHOH2306
BGLU221
BPHE239
BGOL1504

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1501
ChainResidue
BTRP97
BTYR98
BHOH2059
CGOL1502
BPHE12
BPHE51

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1503
ChainResidue
BPRO260
BPHE263
BSER264
BARG439
BTHR441
BHOH2160

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL C 1502
ChainResidue
BGOL1501
CHOH2300

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 1504
ChainResidue
ATRP479
ATYR481
AILE482
AASP489
AGOL1500
BPHE190
BPHE191
BARG194
BHOH2301

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR CHAIN C OF ARGADIN
ChainResidue
ATYR481
BTYR10
BTRP97
BASP142
BGLU144
BPHE191
BMET212
BTYR214
BASP215
BTRP220
BTYR292
BARG294
BASP316
BILE339
BTRP403
BGOL1501
CGOL1502
CHOH2001

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR CHAIN D OF ARGADIN
ChainResidue
ATYR10
ATRP97
AASP142
AGLU144
APHE191
ATYR214
AASP215
ATRP220
ATYR292
AARG294
AASP316
ATRP403
BTYR481
DHOH2005
DHOH2006

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGVDIDwE
ChainResidueDetails
APHE136-GLU144

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AGLU144
BGLU144

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AASP68
BTRP403
AGLY95
ATYR145
AMET212
ATRP403
BASP68
BGLY95
BTYR145
BMET212

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP142
ATYR214
AGLU144

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
BASP142
BTYR214
BGLU144

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP142
AGLU144

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
BASP142
BGLU144

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP140
AGLU144

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
BASP140
BGLU144

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PDB entries from 2025-06-18

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