Structure of PDB 3dxv Chain B

Receptor sequence
>3dxvB (length=434) Species: 37486 (Achromobacter obae) [Search protein sequence]
KALYDRDGAAIGNLQKLRFFPLAISGGRGARLIEENGRELIDLSGAWGAA
SLGYGHPAIVAAVSAAAANPAGATILSASNAPAVTLAERLLASFPGEGTH
KIWFGHSGSDANEAAYRAIVKATGRSGVIAFAGAYHGCTVGSMAFSGHSV
QADAAKADGLILLPYPDPYRPYRNDPTGDAILTLLTEKLAAVPAGSIGAA
FIEPIQSDGGLIVPPDGFLRKFADICRAHGILVVCDEVKVGLARSGRLHC
FEHEGFVPDILVLGKGLGGGLPLSAVIAPAEILDCASAFAMQTLHGNPIS
AAAGLAVLETIDRDDLPAMAERKGRLLRDGLSELAKRHPLIGDIRGRGLA
CGMELVCDRQSREPARAETAKLIYRAYQLGLVVYYVGMNGNVLEFTPPLT
ITETDIHKALDLLDRAFSELSAVSNEEIAQFAGW
3D structure
PDB3dxv The novel structure of a pyridoxal 5'-phosphate-dependent fold-type I racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
ChainB
Resolution2.21 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q17 Y137 E205 D238 K241 K267 T295 E396
Catalytic site (residue number reindexed from 1) Q15 Y135 E203 D236 K239 K265 T293 E394
Enzyme Commision number 5.1.1.15: 2-aminohexano-6-lactam racemase.
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 PLP B Q294 T295 Q292 T293
BS02 PLP B S109 S111 Y137 H138 E205 D238 V240 K267 S107 S109 Y135 H136 E203 D236 V238 K265
Gene Ontology
Molecular Function
GO:0008453 alanine-glyoxylate transaminase activity
GO:0008483 transaminase activity
GO:0016853 isomerase activity
GO:0030170 pyridoxal phosphate binding
GO:0047463 2-aminohexano-6-lactam racemase activity
Biological Process
GO:0009436 glyoxylate catabolic process
GO:0019481 L-alanine catabolic process, by transamination

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Molecular Function

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Biological Process
External links
PDB RCSB:3dxv, PDBe:3dxv, PDBj:3dxv
PDBsum3dxv
PubMed19146406
UniProtQ7M181|ACLR_ACHOB 2-aminohexano-6-lactam racemase

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