Structure of PDB 1pjx Chain A

Receptor sequence
>1pjxA (length=314) Species: 6622 (Loligo vulgaris) [Search protein sequence]
MEIPVIEPLFTKVTEDIPGAEGPVFDKNGDFYIVAPEVEVNGKPAGEILR
IDLKTGKKTVICKPEVNGYGGIPAGCQCDRDANQLFVADMRLGLLVVQTD
GTFEEIAKKDSEGRRMQGCNDCAFDYEGNLWITAPAGEVAPADYTRSMQE
KFGSIYCFTTDGQMIQVDTAFQFPNGIAVRHMNDGRPYQLIVAETPTKKL
WSYDIKGPAKIENKKVWGHIPGTHEGGADGMDFDEDNNLLVANWGSSHIE
VFGPDGGQPKMRIRCPFEKPSNLHFKPQTKTIFVTEHENNAVWKFEWQRN
GKKQYCETLKFGIF
3D structure
PDB1pjx Statistical analysis of crystallographic data obtained from squid ganglion DFPase at 0.85 A resolution.
ChainA
Resolution0.85 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) E21 E37 N120 N175 D229 H287
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 E21 N120 N175 D229
BS02 CA A D232 L273 H274 D232 L273 H274
BS03 DXE A K151 W201 K214 K151 W201 K214
BS04 DXE A W244 K269 W244 K269
BS05 DXE A P8 E296 W297 P8 E296 W297
BS06 MXE A K151 A170 F171 E194 K214 K151 A170 F171 E194 K214
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:1pjx, PDBe:1pjx, PDBj:1pjx
PDBsum1pjx
PubMed14501113
UniProtQ7SIG4|DFPA_LOLVU Diisopropyl-fluorophosphatase

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