Structure of PDB 4izd Chain A

Receptor sequence
>4izdA (length=253) Species: 246200 (Ruegeria pomeroyi DSS-3) [Search protein sequence]
TQDVTSGYSNLDLDLRDNGVCVVTLNRPDKRNALDVATIEELVTFFSTAH
RKGVRAVVLTGAGDHFCAGLDLVEHWKADRSADDFMHVCLRWHEAFNKME
YGGVPIIAALRGAVVGGGLALASAAHLRVMDQSTYFALPEGQRGIFTGGG
ATIRVSDMIGKYRMIDMILTGRVYQGQEAADLGLAQYITEGSSFDKAMEL
ADKIASNLPLTNFAICSAISHMQNMSGLDAAYAEAFVGGIVNTQPAARER
LEA
3D structure
PDB4izd Crystal Structure of DmdD, a Crotonase Superfamily Enzyme That Catalyzes the Hydration and Hydrolysis of Methylthioacryloyl-CoA.
ChainA
Resolution1.8 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) L71 H76 C90 H94 G118 A121 E141 G149 Y233
Catalytic site (residue number reindexed from 1) L70 H75 C89 H93 G117 A120 E140 G148 Y232
Enzyme Commision number 4.2.1.155: methylthioacryloyl-CoA hydratase.
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 1HE A D30 K31 R32 A34 A69 L71 D72 L73 D29 K30 R31 A33 A68 L70 D71 L72
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004300 enoyl-CoA hydratase activity
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
Biological Process
GO:0006635 fatty acid beta-oxidation
GO:0034214 protein hexamerization

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4izd, PDBe:4izd, PDBj:4izd
PDBsum4izd
PubMed23704947
UniProtQ5LLW6|DMDD_RUEPO Methylthioacryloyl-CoA hydratase (Gene Name=dmdD)

[Back to BioLiP]