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1CUD

CUTINASE, N172K, R196D MUTANT, MONOCLINIC CRYSTAL FORM WITH THREE MOLECULES PER ASYMMETRIC UNIT

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016052biological_processcarbohydrate catabolic process
A0016787molecular_functionhydrolase activity
A0050525molecular_functioncutinase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
B0005576cellular_componentextracellular region
B0016052biological_processcarbohydrate catabolic process
B0016787molecular_functionhydrolase activity
B0050525molecular_functioncutinase activity
B0052689molecular_functioncarboxylic ester hydrolase activity
C0005576cellular_componentextracellular region
C0016052biological_processcarbohydrate catabolic process
C0016787molecular_functionhydrolase activity
C0050525molecular_functioncutinase activity
C0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idCAA
Number of Residues3
DetailsCATALYTIC TRIAD, CHAIN A
ChainResidue
ASER120
AASP175
AHIS188

site_idCAB
Number of Residues3
DetailsCATALYTIC TRIAD, CHAIN B
ChainResidue
BSER120
BASP175
BHIS188

site_idCAC
Number of Residues3
DetailsCATALYTIC TRIAD, CHAIN C
ChainResidue
CSER120
CASP175
CHIS188

Functional Information from PROSITE/UniProt
site_idPS00155
Number of Residues13
DetailsCUTINASE_1 Cutinase, serine active site. PdAtLIaGGYSQG
ChainResidueDetails
APRO110-GLY122

site_idPS00931
Number of Residues18
DetailsCUTINASE_2 Cutinase, aspartate and histidine active sites. CktgDlVCtGSliVaapH
ChainResidueDetails
ACYS171-HIS188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8286366","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9041628","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OXM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CUT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8286366","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9041628","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OXM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CUT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1agy
ChainResidueDetails
AASP175
AGLN121
ASER42
ASER120
AHIS188

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1agy
ChainResidueDetails
BASP175
BGLN121
BSER42
BSER120
BHIS188

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1agy
ChainResidueDetails
CASP175
CGLN121
CSER42
CSER120
CHIS188

site_idMCSA1
Number of Residues5
DetailsM-CSA 631
ChainResidueDetails
ASER42electrostatic stabiliser
ASER120covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AGLN121electrostatic stabiliser
AASP175electrostatic stabiliser, increase basicity
AHIS188proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 631
ChainResidueDetails
BSER42electrostatic stabiliser
BSER120covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
BGLN121electrostatic stabiliser
BASP175electrostatic stabiliser, increase basicity
BHIS188proton acceptor, proton donor

site_idMCSA3
Number of Residues5
DetailsM-CSA 631
ChainResidueDetails
CSER42electrostatic stabiliser
CSER120covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
CGLN121electrostatic stabiliser
CASP175electrostatic stabiliser, increase basicity
CHIS188proton acceptor, proton donor

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PDB entries from 2025-10-08

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