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9FYU

Crystal structure of the engineered photoenzyme VEnT1.0

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0047862molecular_functiondiisopropyl-fluorophosphatase activity
B0005509molecular_functioncalcium ion binding
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0047862molecular_functiondiisopropyl-fluorophosphatase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15966726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11435114","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14501113","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 686
ChainResidueDetails
AALA21increase nucleophilicity, metal ligand, proton acceptor
ATYR37electrostatic stabiliser, increase basicity
AALA120metal ligand
AHIS181metal ligand
AGLU235covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor
ATRP293increase nucleophilicity, proton acceptor

site_idMCSA2
Number of Residues6
DetailsM-CSA 686
ChainResidueDetails
BALA21increase nucleophilicity, metal ligand, proton acceptor
BTYR37electrostatic stabiliser, increase basicity
BALA120metal ligand
BHIS181metal ligand
BGLU235covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor
BTRP293increase nucleophilicity, proton acceptor

242500

PDB entries from 2025-10-01

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