Structure of PDB 4rlh Chain D

Receptor sequence
>4rlhD (length=253) Species: 272560 (Burkholderia pseudomallei K96243) [Search protein sequence]
MGFLDGKRILLTGLLSNRSIAYGIAKACKREGAELAFTYVGDRFKDRITE
FAAEFGSELVFPCDVADDAQIDALFASLKTHWDSLDGLVHSIGFAPREAI
AGDFLDGLTRENFRIAHDISAYSFPALAKAALPMLSDDASLLTLSYLGAE
RAIPNYNTMGLAKAALEASVRYLAVSLGAKGVRVNAISAGPISGIKSFGK
ILDFVESNSPLKRNVTIEQVGNAGAFLLSDLASGVTAEVMHVDSGFNAVV
GGM
3D structure
PDB4rlh Crystal structure of enoyl ACP reductase from Burkholderia pseudomallei in complex with AFN-1252
ChainD
Resolution2.26 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y156 K163
Catalytic site (residue number reindexed from 1) Y156 K163
Enzyme Commision number 1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH).
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 0WE D F94 A95 R97 I100 Y146 N155 Y156 F203 F94 A95 R97 I100 Y146 N155 Y156 F198
Gene Ontology
Molecular Function
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4rlh, PDBe:4rlh, PDBj:4rlh
PDBsum4rlh
PubMed
UniProtQ63SW7

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