Structure of PDB 5vm2 Chain A

Receptor sequence
>5vm2A (length=347) Species: 562 (Escherichia coli) [Search protein sequence]
MKNSKAILQVPGTMKIISAEIPVPKEDEVLIKVEYVGICGSDVHGFESGP
FIPPKDPNQEIGLGHECAGTVVAVGSRVRKFKPGDRVNIEPGVPCGHCRY
CLEGKYNICPDVDFMATQPNYRGALTHYLCHPESFTYKLPDNMDTMEGTL
VEPAAVGMHAAMLADVKPGKKIIILGAGCIGLMTLQACKCLGATEIAVVD
VLEKRLAMAEQLGATVVINGAKEDTIARCQQFTEDMGADIVFETAGSAVT
VKQAPYLVMRGGKIMIVGTVPGASAINFLKINREVTIQTVFRYANRYPVT
IEAISSGRFDVKSMVTHIYDYRDVQQAFEESVNNKRDIIKGVIKISD
3D structure
PDB5vm2 Crystal structure of ECK1772, an oxidoreductase/dehydrogenase of unknown specificity involved in membrane biogenesis from Escherichia coli
ChainA
Resolution1.983 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) C39 G40 S41 H44 H65 E66 C95 C98 C101 C109 D113 P153 G157 K340
Catalytic site (residue number reindexed from 1) C39 G40 S41 H44 H65 E66 C95 C98 C101 C109 D113 P153 G157 K340
Enzyme Commision number 1.-.-.-
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 MG A H65 E66 E152 H65 E66 E152
BS02 ZN A C95 C98 C101 C109 C95 C98 C101 C109
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:5vm2, PDBe:5vm2, PDBj:5vm2
PDBsum5vm2
PubMed
UniProtP77280|YDJJ_ECOLI Uncharacterized zinc-type alcohol dehydrogenase-like protein YdjJ (Gene Name=ydjJ)

[Back to BioLiP]