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7ZP7

Crystal structure of evolved photoenzyme EnT1.3 (truncated) with bound product

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0008150biological_processbiological_process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0047862molecular_functiondiisopropyl-fluorophosphatase activity
B0005509molecular_functioncalcium ion binding
B0008150biological_processbiological_process
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0047862molecular_functiondiisopropyl-fluorophosphatase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:15966726
ChainResidueDetails
AHIS287
BHIS287

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AALA21
AALA120
AALA175
ASER229
BALA21
BALA120
BALA175
BSER229

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11435114, ECO:0000269|PubMed:14501113
ChainResidueDetails
AASP232
ALEU273
AHIS274
BASP232
BLEU273
BHIS274

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
AALA175metal ligand
ASER229covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor
AHIS287increase nucleophilicity, proton acceptor

site_idMCSA2
Number of Residues6
DetailsM-CSA 686
ChainResidueDetails
BALA21increase nucleophilicity, metal ligand, proton acceptor
BTYR37electrostatic stabiliser, increase basicity
BALA120metal ligand
BALA175metal ligand
BSER229covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor
BHIS287increase nucleophilicity, proton acceptor

223532

PDB entries from 2024-08-07

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