Structure of PDB 2zuk Chain A

Receptor sequence

>2zukA (length=422) Species: 37486 (Achromobacter obae)

TKALYDRDGAAIGNLQKLRFFPLAISGGRGARLIEENGRELIDLSGAWGA
ASLGYGHPAIVAAVSAAAANPAGATILSASNAPAVTLAERLLASFPGEGT
HKIWFGHSGSDANEAAYRAIVKATGRSGVIAFAGAYHGCTVGSMAFGLIL
LPYPDPYRPYRNDPTGDAILTLLTEKLAAVPAGSIGAAFIEPIQSDGGLI
VPPDGFLRKFADICRAHGILVVCDEVKVGLARSGRLHCFEHEGFVPDILV
LGKGLGGGLPLSAVIAPAEILDCASAFAMQTLHGNPISAAAGLAVLETID
RDDLPAMAERKGRLLRDGLSELAKRHPLIGDIRGRGLACGMELVCDRQSR
EPARAETAKLIYRAYQLGLVVYYVGMNGNVLEFTPPLTITETDIHKALDL
LDRAFSELSAVSNEEIAQFAGW

3D structure

• PDB: 2zuk The novel structure of a pyridoxal 5'-phosphate-dependent fold-type I racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
• Chain: A
• 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): 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	ICC	A	L19 W49 Y137 K241 K267 W436	L18 W48 Y136 K227 K253 W422
BS02	PLP	A	G110 S111 Y137 H138 D238 V240 K267	G109 S110 Y136 H137 D224 V226 K253
BS03	ICC	A	L78 T295	L77 T281
BS04	PLP	A	Q294 T295	Q280 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

External links

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