Structure of PDB 2imq Chain X

Receptor sequence
>2imqX (length=280) Species: 79782 (Cimex lectularius) [Search protein sequence]
PPAQLSVHTVSWNSGHERAPTNLEELLGLNSGETPDVIAVAVQGFGFQTD
KPQQGPACVKNFQSLLTSKGYTKLKNTITETMGLTVYCLEKHLDQNTLKN
ETIIVTVDDQKKSGGIVTSFTIYNKRFSFTTSRMSDEDVTSTNTKYAYDT
RLDYSKKDDPSDFLFWIGDLNVRVETNATHAKSLVDQNNIDGLMAFDQLK
KAKEQKLFDGWTEPQVTFKPTYKFKPNTDEYDLSATPSWTDRALYKSGTG
KTIQPLSYNSLTNYKQTEHRPVLAKFRVTL
3D structure
PDB2imq Heme-assisted S-nitrosation of a proximal thiolate in a nitric oxide transport protein
ChainX
Resolution1.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 HEM X W14 S16 E19 A21 V44 G48 F49 D52 Q56 G57 C60 V61 F64 Q65 K75 N78 I80 T87 Y89 W12 S14 E17 A19 V42 G46 F47 D50 Q54 G55 C58 V59 F62 Q63 K73 N76 I78 T85 Y87
Gene Ontology
Molecular Function
GO:0004439 phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity
GO:0005506 iron ion binding
GO:0016791 phosphatase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0030185 nitric oxide transport
GO:0042311 vasodilation
GO:0044552 vasodilation in another organism
GO:0046856 phosphatidylinositol dephosphorylation
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2imq, PDBe:2imq, PDBj:2imq
PDBsum2imq
PubMed
UniProtO76745|NP_CIMLE Nitrophorin Cim l NP

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