Structure of PDB 2ahv Chain D

Receptor sequence
>2ahvD (length=512) Species: 83334 (Escherichia coli O157:H7) [Search protein sequence]
VKPPRINGRVPVLSAQEAVNYIPDEATLCVLGAGGGILEATTLITALADK
YKQTQTPRNLSIISPTGLGDRADRGISPLAQEGLVKWALCGHWGQSPRIS
DLAEQNKIIAYNYPQGVLTQTLRAAAAHQPGIISDIGIGTFVDPRQQGGK
LNEVTKEDLIKLVEFDNKEYLYYKAIAPDIAFIRATTCDSEGYATFEDEV
MYLDALVIAQAVHNNGGIVMMQVQKMVKKATLHPKSVRIPGYLVDIVVVD
PDQSQLYGGAPVNRFISGDFTLDPLNQRKLVARRALFEMRKGAVGNVGVG
IADGIGLVAREEGCADDFILTVETGPIGGITANVNTRAILDMTSQFDFYH
GGGLDVCYLSFAEVDQHGNVGVHKFNGKIMGTGGFIDISATSKKIIFCGT
LTAGSLKTEIADGKLNIVQEGRVKKFIRELPEITFSGKIALERGLDVRYI
TERAVFTLKEDGLHLIEIAPGVDLQKDILDKMDFTPVISPELKLMDERLF
IDAAMGFVLPEA
3D structure
PDB2ahv Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases.
ChainD
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.8.3.8: acetate CoA-transferase.
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 COA D R288 G310 I311 E333 L376 S377 A379 F392 N393 T399 F402 R278 G300 I301 E323 L359 S360 A362 F375 N376 T382 F385
Gene Ontology
Molecular Function
GO:0008410 CoA-transferase activity
GO:0008775 acetate CoA-transferase activity
GO:0016740 transferase activity
Biological Process
GO:0046459 short-chain fatty acid metabolic process
GO:0046952 ketone body catabolic process
GO:0051289 protein homotetramerization

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2ahv, PDBe:2ahv, PDBj:2ahv
PDBsum2ahv
PubMed16253988
UniProtQ8X5X6|YDIF_ECO57 Acetate CoA-transferase YdiF (Gene Name=ydiF)

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