Structure of PDB 4rvo Chain A

Receptor sequence
>4rvoA (length=434) Species: 226186 (Bacteroides thetaiotaomicron VPI-5482) [Search protein sequence]
GMSTQYWEEEIEIMSREKLQELQLQRLKKTINIAANSPYYKEVFSKNGIT
GDSIQSLDDIRKIPFTTKSDMRANYPFGLVAGDMKRDGVRIHSSSGTTGN
PTVIVHSQHDLDSWANLVARCLYMVGIRKTDVFQNSSGYGMFTGGLGFQY
GAERLGCLTVPAAAGNSKRQIKFISDFKTTALHAIPSYAIRLAEVFQEEG
IDPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMNGPGVAF
ECQEQNGMHFWEDCYLVEIIDPETGEPVPEGEIGELVLTTLDREMMPLIR
YRTRDLTRILPGKCPCGRTHLRIDRIKGRSDDMFIIKGVNIFPMQVEKIL
VQFPELGSNYLITLETVNNQDEMIVEVELSDLSTDNYIELEKIRRDIIRQ
LKDEILVTPKVKLVKKGSLPQSEGKAVRVKDLRD
3D structure
PDB4rvo Crystal structure of a Putative Acyl-CoA ligase (BT_0428) from Bacteroides thetaiotaomicron VPI-5482 at 2.41 A resolution
ChainA
Resolution2.41 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.2.1.30: phenylacetate--CoA ligase.
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 ZN A C251 H258 C313 C315 C252 H259 C314 C316
BS02 ADP A A214 E215 P216 S236 F237 G238 M239 T240 D304 R328 N339 A215 E216 P217 S237 F238 G239 M240 T241 D305 R329 N340
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
GO:0047475 phenylacetate-CoA ligase activity
Biological Process
GO:0010124 phenylacetate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4rvo, PDBe:4rvo, PDBj:4rvo
PDBsum4rvo
PubMed
UniProtQ8AAN6

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