Structure of PDB 3dxw Chain B

Receptor sequence

>3dxwB (length=426) Species: 37486 (Achromobacter obae)

KALYDRDGAAIGNLQKLRFFPLAISGGRGARLIEENGRELIDLSGAWGAA
SLGYGHPAIVAAVSAAAANPAGATILSASNAPAVTLAERLLASFPGEGTH
KIWFGHSGSDANEAAYRAIVKATGRSGVIAFAGAYHGCTVGSMAFSGHAD
GLILLPYPDPYRPYRNDPTGDAILTLLTEKLAAVPAGSIGAAFIEPIQSD
GGLIVPPDGFLRKFADICRAHGILVVCDEVKVGLARSGRLHCFEHEGFVP
DILVLGKGLGGGLPLSAVIAPAEILDCASAFAMQTLHGNPISAAAGLAVL
ETIDRDDLPAMAERKGRLLRDGLSELAKRHPLIGDIRGRGLACGMELVCD
RQSREPARAETAKLIYRAYQLGLVVYYVGMNGNVLEFTPPLTITETDIHK
ALDLLDRAFSELSAVSNEEIAQFAGW

3D structure

• PDB: 3dxw The novel structure of a pyridoxal 5'-phosphate-dependent fold-type I racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
• Chain: B
• Resolution: 2.41 Å

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 E195 D228 K231 K257 T285 E386
• 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	Q284 T285
BS02	PLP	B	S109 G110 S111 Y137 H138 E205 D238 V240 K267	S107 G108 S109 Y135 H136 E195 D228 V230 K257
BS03	ICC	B	L19 W49 K267 W436	L17 W47 K257 W426

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

External links

• PDB: RCSB:3dxw, PDBe:3dxw, PDBj:3dxw
• PDBsum: 3dxw
• PubMed: 19146406
• UniProt: Q7M181|ACLR_ACHOB 2-aminohexano-6-lactam racemase