Structure of PDB 1wdl Chain D

Receptor sequence
>1wdlD (length=390) Species: 296 (Pseudomonas fragi) [Search protein sequence]
SLNPRDVVIVDFGRTPMGRSKGGMHRNTRAEDMSAHLISKVLERNSKVDP
GEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHTSAAQTVSRLCGSSMSA
LHTAAQAIMTGNGDVFVVGGVEHMGHVSMMHGVDPNPHMSLYAAKASGMM
GLTAEMLGKMHGISREQQDAFAVRSHQLAHKATVEGKFKDEIIPMQGYDE
NGFLKIFDYDETIRPDTTLESLAALKPAFNPKGGTVTAGTSSQITDGASC
MIVMSAQRAKDLGLEPLAVIRSMAVAGVDPAIMGYGPVPATQKALKRAGL
NMADIDFIELNEAFAAQALPVLKDLKVLDKMNEKVNLHGGAIALGHPFGC
SGARISGTLLNVMKQNGGTFGLSTMCIGLGQGIATVFERV
3D structure
PDB1wdl Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex
ChainD
Resolution3.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C95 H347 C377 G379
Catalytic site (residue number reindexed from 1) C94 H346 C376 G378
Enzyme Commision number 2.3.1.16: acetyl-CoA C-acyltransferase.
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 ACO D C95 M151 R215 T218 L223 A239 S243 M284 A314 F315 H347 F349 C377 C94 M150 R214 T217 L222 A238 S242 M283 A313 F314 H346 F348 C376
Gene Ontology
Molecular Function
GO:0003988 acetyl-CoA C-acyltransferase activity
GO:0005515 protein binding
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
GO:0010124 phenylacetate catabolic process
GO:0016042 lipid catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1wdl, PDBe:1wdl, PDBj:1wdl
PDBsum1wdl
PubMed15229654
UniProtP28790|FADA_PSEFR 3-ketoacyl-CoA thiolase (Gene Name=fadA)

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