Structure of PDB 4rvn Chain D

Receptor sequence
>4rvnD (length=426) Species: 226186 (Bacteroides thetaiotaomicron VPI-5482) [Search protein sequence]
STQYWEEEIEIMSREKLQELQLQRLKKTINIAANSPYYKEVFSKNGITGD
SIQSLDDIRKIPFTTKSDMRANYPFGLVAGDMKRDGVRIHSSNPTVIVHS
QHDLDSWANLVARCLYMVGIRKTDVFQNSSGYGMFTGGLGFQYGAERLGC
LTVPAAAGNSKRQIKFISDFKTTALHAIPSYAIRLAEVFQEEGIDPRETT
LKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMNGPGVAFECQEQNG
MHFWEDCYLVEIIDPETGEPVPEGEIGELVLTTLDREMMPLIRYRTRDLT
RILPGKCPCGRTHLRIDRIKGRSDDMFIIKGVNIFPMQVEKILVQFPELG
SNYLITLETNQDEMIVEVELSDLSTDNYIELEKIRRDIIRQLKDEILVTP
KVKLVKKGSLPQSEGKAVRVKDLRDN
3D structure
PDB4rvn Crystal structure of a Putative Acyl-CoA ligase (BT_0428) from Bacteroides thetaiotaomicron VPI-5482 at 2.20 A resolution
ChainD
Resolution2.2 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 D C251 H258 C313 C315 C245 H252 C307 C309
BS02 AMP D A214 P216 S236 F237 G238 M239 T240 D304 I325 R328 K424 A208 P210 S230 F231 G232 M233 T234 D298 I319 R322 K416
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

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:4rvn, PDBe:4rvn, PDBj:4rvn
PDBsum4rvn
PubMed
UniProtQ8AAN6

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