Structure of PDB 2d3t Chain D

Receptor sequence
>2d3tD (length=390) Species: 296 (Pseudomonas fragi) [Search protein sequence]
SLNPRDVVIVDFGRTPMGRSKGGMHRNTRAEDMSAHLISKVLERNSKVDP
GEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHTSAAQTVSRLCGSSMSA
LHTAAQAIMTGNGDVFVVGGVEHMGHVSMMHGVDPNPHMSLYAAKASGMM
GLTAEMLGKMHGISREQQDAFAVRSHQLAHKATVEGKFKDEIIPMQGYDE
NGFLKIFDYDETIRPDTTLESLAALKPAFNPKGGTVTAGTSSQITDGASC
MIVMSAQRAKDLGLEPLAVIRSMAVAGVDPAIMGYGPVPATQKALKRAGL
NMADIDFIELNEAFAAQALPVLKDLKVLDKMNEKVNLHGGAIALGHPFGC
SGARISGTLLNVMKQNGGTFGLSTMCIGLGQGIATVFERV
3D structure
PDB2d3t Ligand-Induced Domain Rearrangement of Fatty Acid beta-Oxidation Multienzyme Complex
ChainD
Resolution3.4 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 T218 S222 L223 L226 F230 S243 A314 F315 H347 C377 C94 M150 T217 S221 L222 L225 F229 S242 A313 F314 H346 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:2d3t, PDBe:2d3t, PDBj:2d3t
PDBsum2d3t
PubMed16472743
UniProtP28790|FADA_PSEFR 3-ketoacyl-CoA thiolase (Gene Name=fadA)

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