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2O7V

Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
A0106435molecular_functioncarboxylesterase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DEP A 401
ChainResidue
AGLY92
AGLY93
ASER169
AALA170
ATRP231
AMET278
AHIS306

Functional Information from PROSITE/UniProt
site_idPS01173
Number of Residues17
DetailsLIPASE_GDXG_HIS Lipolytic enzymes "G-D-X-G" family, putative histidine active site. VVyFHGGGFilfSaaST
ChainResidueDetails
AVAL86-THR102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000305
ChainResidueDetails
ASER169
AASP276
AHIS306

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:17256879, ECO:0007744|PDB:2O7V
ChainResidueDetails
AGLY92
AALA170

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: covalent => ECO:0000305|PubMed:17256879, ECO:0007744|PDB:2O7V
ChainResidueDetails
ASER169

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jkm
ChainResidueDetails
AHIS306
AASP276
ASER169

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PDB entries from 2024-07-17

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