Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1CUV

CUTINASE, A85F MUTANT

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0050525molecular_functioncutinase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idCAT
Number of Residues3
DetailsCATALYTIC TRIAD
ChainResidue
ASER120
AHIS188
AASP175

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. CntgDlVCtGSliVaapH
ChainResidueDetails
ACYS171-HIS188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY
ChainResidueDetails
ASER120

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY
ChainResidueDetails
AASP175

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY
ChainResidueDetails
AHIS188

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:1560844, ECO:0000269|PubMed:8286366, ECO:0000269|PubMed:8555209, ECO:0000269|PubMed:9041628, ECO:0007744|PDB:1AGY, ECO:0007744|PDB:1FFE, ECO:0007744|PDB:1OXM, ECO:0007744|PDB:2CUT
ChainResidueDetails
ASER42

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:1560844, ECO:0000269|PubMed:8286366, ECO:0000269|PubMed:9041628, ECO:0007744|PDB:1AGY, ECO:0007744|PDB:1OXM, ECO:0007744|PDB:2CUT
ChainResidueDetails
AGLN121

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-D-glucuronoyl glycine => ECO:0000269|PubMed:7398618
ChainResidueDetails
AGLY16

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

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon