Structure of PDB 1ps9 Chain A

Receptor sequence

>1ps9A (length=671) Species: 562 (Escherichia coli) [Search protein sequence]

SYPSLFAPLDLGFTTLKNRVLMGSMHTGLEEYPDGAERLAAFYAERARHG
VALIVSGGIAPDLTGVGMEGGAMLNDASQIPHHRTITEAVHQEGGKIALQ
ILHTGRYSYQPHLVAPSALQAPINRFVPHELSHEEILQLIDNFARCAQLA
REAGYDGVEVMGSEGYLINEFLTLRTNQRSDQWGGDYRNRMRFAVEVVRA
VRERVGNDFIIIYRLSMLDLVEDGGTFAETVELAQAIEAAGATIINTGIG
WHEARIPTIATPVPRGAFSWVTRKLKGHVSLPLVTTNRINDPQVADDILS
RGDADMVSMARPFLADAELLSKAQSGRADEINTCIGCNQACLDQIFVGKV
TSCLVNPRACHETKMPILPAVQKKNLAVVGAGPAGLAFAINAAARGHQVT
LFDAHSEIGGQFNIAKQIPGKEEFYETLRYYRRMIEVTGVTLKLNHTVTA
DQLQAFDETILASGIVPRTPPIDGIDHPKVLSYLDVLRDKAPVGNKVAII
GCGGIGFDTAMYLSQPGESTSQNIAGFCNEWGIDSSLQQAGGLSPQGMQI
PRSPRQIVMLQRKASKPGQGLGKTTGWIHRTTLLSRGVKMIPGVSYQKID
DDGLHVVINGETQVLAVDNVVICAGQEPNRALAQPLIDSGKTVHLIGGCD
VAMELDARRAIAQGTRLALEI

3D structure

PDB

1ps9 The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase

Chain

Resolution

2.2 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	H26 M161 E164 Y166 R214 E222 H252 Q339
Catalytic site (residue number reindexed from 1)	H26 M161 E164 Y166 R214 E222 H252 Q339
Enzyme Commision number	1.3.1.34: 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing].

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	SF4	A	R311 C334 I335 G336 C337 N338 C341 C353 L354	R311 C334 I335 G336 C337 N338 C341 C353 L354
BS02	FAD	A	Q339 G380 G382 P383 A384 D403 H405 G410 Q411 F412 I414 A415 I418 K421 F424 V448 G464 D508 G647 G648 D656 A657	Q339 G380 G382 P383 A384 D403 H405 G410 Q411 F412 I414 A415 I418 K421 F424 V448 G464 D508 G647 G648 D656 A657
BS03	FMN	A	S24 M25 H26 G58 Q100 M161 R214 R288 A310 R311 C341	S24 M25 H26 G58 Q100 M161 R214 R288 A310 R311 C341
BS04	NAP	A	Q339 R468 G504 I505 Q561 R562 K563 L571 A624 G625 E654 L655 D656	Q339 R468 G504 I505 Q561 R562 K563 L571 A624 G625 E654 L655 D656
BS05	MDE	A	H26 L102 P122 E164 Y166 H252 E253 I259 L342 F346 T574 W577	H26 L102 P122 E164 Y166 H252 E253 I259 L342 F346 T574 W577

Gene Ontology

	Molecular Function
GO:0005515	protein binding
GO:0008670	2,4-dienoyl-CoA reductase (NADPH) activity
GO:0010181	FMN binding
GO:0016491	oxidoreductase activity
GO:0046872	metal ion binding
GO:0051539	4 iron, 4 sulfur cluster binding
GO:0071949	FAD binding

	Biological Process
GO:0006635	fatty acid beta-oxidation
GO:0009056	catabolic process
GO:0033543	fatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathway

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:1ps9, PDBe:1ps9, PDBj:1ps9
PDBsum	1ps9
PubMed	12840019
UniProt	P42593\|FADH_ECOLI 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing] (Gene Name=fadH)

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