Structure of PDB 2iaq Chain A

Receptor sequence
>2iaqA (length=312) Species: 6622 (Loligo vulgaris) [Search protein sequence]
IPVIEPLFTKVTEDIPGAEGPVFDKNGDFYIVAPEVEVNGKPAGEILRID
LKTGKKTVICKPEVNGYGGIPAGCQCDRDANQLFVADMRLGLLVVQTDGT
FEEIAKKDSEGRRMQGCNDCAFDYEGNLWITAPAGEVAPADYTRSMQEKF
GSIYCFTTDGQMIQVDTAFQFPNGIAVRHMNDGRPYQLIVAETPTKKLWS
YDIKGPAKIENKKVWGHIPGTHEGGADGMDFDEDNNLLVANWGSSHIEVF
GPDGGQPKMRIRCPFEKPANLHFKPQTKTIFVTEHENNAVWKFEWQRNGK
KQYCETLKFGIF
3D structure
PDB2iaq Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E21 E37 N120 N175 D229 H287
Catalytic site (residue number reindexed from 1) E19 E35 N118 N173 D227 H285
Enzyme Commision number 3.8.2.2: diisopropyl-fluorophosphatase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA A E21 N120 N175 D229 E19 N118 N173 D227
BS02 CA A D232 L273 H274 D230 L271 H272
Gene Ontology
Molecular Function
GO:0005509 calcium ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0047862 diisopropyl-fluorophosphatase activity
Biological Process
GO:0008150 biological_process

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Molecular Function
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Biological Process
External links
PDB RCSB:2iaq, PDBe:2iaq, PDBj:2iaq
PDBsum2iaq
PubMed11435114
UniProtQ7SIG4|DFPA_LOLVU Diisopropyl-fluorophosphatase

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