Structure of PDB 3dxw Chain A

Receptor sequence
>3dxwA (length=422) Species: 37486 (Achromobacter obae) [Search protein sequence]
TKALYDRDGAAIGNLQKLRFFPLAISGGRGARLIEENGRELIDLSGAWGA
ASLGYGHPAIVAAVSAAAANPAGATILSASNAPAVTLAERLLASFPGEGT
HKIWFGHSGSDANEAAYRAIVKATGRSGVIAFAGAYHGCTVGSMAFGLIL
LPYPDPYRPYRNDPTGDAILTLLTEKLAAVPAGSIGAAFIEPIQSDGGLI
VPPDGFLRKFADICRAHGILVVCDEVKVGLARSGRLHCFEHEGFVPDILV
LGKGLGGGLPLSAVIAPAEILDCASAFAMQTLHGNPISAAAGLAVLETID
RDDLPAMAERKGRLLRDGLSELAKRHPLIGDIRGRGLACGMELVCDRQSR
EPARAETAKLIYRAYQLGLVVYYVGMNGNVLEFTPPLTITETDIHKALDL
LDRAFSELSAVSNEEIAQFAGW
3D structure
PDB3dxw The novel structure of a pyridoxal 5'-phosphate-dependent fold-type I racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
ChainA
Resolution2.41 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) Q16 Y136 E191 D224 K227 K253 T281 E382
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 A G110 S111 Y137 H138 D238 V240 K267 G109 S110 Y136 H137 D224 V226 K253
BS02 ICC A L19 W49 K267 W436 L18 W48 K253 W422
BS03 PLP A Q294 T295 Q280 T281
BS04 ICC A L78 T295 L77 T281
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:3dxw, PDBe:3dxw, PDBj:3dxw
PDBsum3dxw
PubMed19146406
UniProtQ7M181|ACLR_ACHOB 2-aminohexano-6-lactam racemase

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