Structure of PDB 6tqh Chain A

Receptor sequence

>6tqhA (length=869) Species: 562 (Escherichia coli) [Search protein sequence]

MAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLA
KMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGVLSEDDTFGTITI
AEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAA
DIVLQAAIAAGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVK
AAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICASEQ
SVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQP
AYKIAELAGFSVPENTKILIGEVTVVDESEPFAHEKLSPTLAMYRAKDFE
DAVEKAEKLVAMGGIGHTSCLYTDQDNQPARVSYFGQKMKTARILINTPA
SQGGIGDLYNFKLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKRAEN
MLWHKLPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQIT
SVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVIIALGGGSPMD
AAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSG
TGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFG
GLDAVTHAMEAYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVAR
ERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLICNVIR
YNANDNPTKQTAFSQYDRPQARRRYAEIADHLGLSAPGDRTAAKIEKLLA
WLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQCTGANPRYPL
ISELKQILLDTYYGRDYVE

3D structure

PDB

6tqh Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation.

Chain

Resolution

3.4 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

1.1.1.1: alcohol dehydrogenase.
1.2.1.10: acetaldehyde dehydrogenase (acetylating).

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)
BS01	NAD	A	D487 F489 G545 G546 S547 T597 T598 T601 S603 T606 F608 V610 K619 M642 L646 H657 F714 H723 H737	D487 F489 G545 G546 S547 T597 T598 T601 S603 T606 F608 V610 K619 M642 L646 H657 F714 H723 H737
BS02	NAD	A	T113 H139 S178 T193 G194 M198 A201 V212 A214 C246 E335 T418 L419	T113 H139 S178 T193 G194 M198 A201 V212 A214 C246 E335 T418 L419
BS03	FE	A	D653 H657 H723 H737	D653 H657 H723 H737

Gene Ontology

	Molecular Function
GO:0004022	alcohol dehydrogenase (NAD+) activity
GO:0005515	protein binding
GO:0008198	ferrous iron binding
GO:0008774	acetaldehyde dehydrogenase (acetylating) activity
GO:0016491	oxidoreductase activity
GO:0016616	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016620	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0018455	alcohol dehydrogenase [NAD(P)+] activity
GO:0042802	identical protein binding
GO:0046872	metal ion binding

	Biological Process
GO:0006066	alcohol metabolic process
GO:0006115	ethanol biosynthetic process
GO:0006979	response to oxidative stress
GO:0015976	carbon utilization
GO:0019664	mixed acid fermentation
GO:0051260	protein homooligomerization

	Cellular Component
GO:0005829	cytosol
GO:0016020	membrane

View graph for
Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:6tqh, PDBe:6tqh, PDBj:6tqh
PDBsum	6tqh
PubMed	32188856
UniProt	P0A9Q7\|ADHE_ECOLI Bifunctional aldehyde-alcohol dehydrogenase AdhE (Gene Name=adhE)

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