Structure of PDB 4nv5 Chain B

Receptor sequence
>4nv5B (length=262) Species: 321332 (Synechococcus sp. JA-2-3B'a(2-13)) [Search protein sequence]
TWLQRHSRLILAILAGLGSLLTAYLTYTKLTEQPAAGGCDLVLSSRWAEF
LGIPTAAVGLLGFLGVLALAVLPDGLPLVKRWRWPALFGLVSAMTAFEMY
MLYLMVAVLRQFCMYCTTAIILVAGLGLVTVLGHRWLDGGKLAFSYILVA
FLTLVTTIGVYANQVPPPSPLAVGLAAHLRQIGGTMYGAYWCPHCQDQKE
LFGAAFDQVPYVECSPNGPGTPQAQECTEAGITSYPTWIINGRTYTGVRS
LEALAVASGYPL
3D structure
PDB4nv5 Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer.
ChainB
Resolution2.79 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 1.17.4.-
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 U10 B V59 L60 A65 G76 A110 M111 F114 E115 M118 M122 C133 I137 V42 L43 A48 G59 A93 M94 F97 E98 M101 M105 C116 I120
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0048038 quinone binding
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function

View graph for
Cellular Component
External links
PDB RCSB:4nv5, PDBe:4nv5, PDBj:4nv5
PDBsum4nv5
PubMed24477003
UniProtQ2JJF6|VKOR_SYNJB Vitamin K epoxide reductase homolog (Gene Name=CYB_2278)

[Back to BioLiP]