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2IAO

Crystal structure of squid ganglion DFPase E37Q mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0008150biological_processbiological_process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0047862molecular_functiondiisopropyl-fluorophosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AGLU21
AASN120
AASN175
AASP229
AHOH501
AHOH526
AHOH614

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AHIS274
AHOH508
AHOH625
AHOH633
AASP232
ALEU273

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:15966726
ChainResidueDetails
AHIS287

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AGLU21
AASN120
AASN175
AASP229

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11435114, ECO:0000269|PubMed:14501113
ChainResidueDetails
AASP232
AHIS274
ALEU273

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 686
ChainResidueDetails
AGLU21increase nucleophilicity, metal ligand, proton acceptor
AGLN37electrostatic stabiliser, increase basicity
AASN120metal ligand
AASN175metal ligand
AASP229covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor
AHIS287increase nucleophilicity, proton acceptor

221051

PDB entries from 2024-06-12

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