Structure of PDB 1yjh Chain A

Receptor sequence
>1yjhA (length=280) Species: 79782 (Cimex lectularius) [Search protein sequence]
PPAQLSVHTVSWNSGHERAPTNLEELLGLNSGETPDVIAVAVQGFGFQTD
KPQQGPACVKNFQSLLTSKGYTKLKNTITETMGLTVYCLEKHLDQNTLKN
ETIIVTVDDQKKSGGIVTSFTIYNKRFSFTTSRMSDEDVTSTNTKYAYDT
RLDYSKKDDPSDFLFWIGDLNVRVETNATHAKSLVDQNNIDGLMAFDQLK
KAKEQKLFDGWTEPQVTFKPTYKFKPNTDEYDLSATPSWTDRALYKSGTG
KTIQPLSYNSLTNYKQTEHRPVLAKFRVTL
3D structure
PDB1yjh Heme-assisted S-nitrosation of a proximal thiolate in a nitric oxide transport protein
ChainA
Resolution1.65 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 A W14 E19 A21 V44 G48 F49 D52 P54 G57 C60 V61 F64 Q65 K75 N78 I80 T87 Y89 W12 E17 A19 V42 G46 F47 D50 P52 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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1yjh, PDBe:1yjh, PDBj:1yjh
PDBsum1yjh
PubMed
UniProtO76745|NP_CIMLE Nitrophorin Cim l NP

[Back to BioLiP]