Structure of PDB 2oas Chain B

Receptor sequence
>2oasB (length=427) Species: 211586 (Shewanella oneidensis MR-1) [Search protein sequence]
PAIVCQSALEAVSLIRSGETLWTHSMGATPKVLLDALAKHALTLDNITLL
QLHTEGAESLSHPSLLGHLRHRCFFGGVPTRPLLQSGDADYVPIFLSEVP
KLFRSGEQKIDTAIIQVSPPDKHGMCSLGISVEATLAACQVAGKIIAHIN
PQMPRTHGDGFIHIDRFAAVYEQSASLPIHSFATGDAVSLAIGQHVAELV
RDGDCLQMGIGAIPDAVLSCLTGHKDLGVHTELFSDGILQLVEKGVINNT
KKRFYPGKLVTGFALGSQKLYDYVDDNPAVIFMDIEQVNDTSIIRKNPNV
MAINSALQVDLTGQVCADSIGTKIYSGVGGQMDFIRGAGLSEGGRSVIAL
PSTAAGGRISRIASVLSPGAGVVTTRAHVHYIVTEYGAANLKGRSLRERA
QALINIAHPDFREQLSRDAFEVWGLNL
3D structure
PDB2oas Crystal Structure of 4-hydroxybutyrate coenzyme A transferase (AtoA) from Shewanella oneidensis in complex with CoA, Northeast Structural Genomics Target SoR119.
ChainB
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 B F76 E233 S306 A307 L308 A318 I321 Y326 S327 G330 G331 Q332 A355 R362 F75 E232 S305 A306 L307 A317 I320 Y325 S326 G329 G330 Q331 A354 R361
Gene Ontology
Molecular Function
GO:0008410 CoA-transferase activity
GO:0008775 acetate CoA-transferase activity
GO:0016740 transferase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006083 acetate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2oas, PDBe:2oas, PDBj:2oas
PDBsum2oas
PubMed
UniProtQ8EG98

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