Structure of PDB 5wya Chain A

Receptor sequence
>5wyaA (length=439) Species: 1581 (Lentilactobacillus buchneri) [Search protein sequence]
KLDKASKLIDEENKYYARSARINYYNLVIDHAHGATLVDVDGNKYIDLLA
SASAINVGHTHEKVVKAIADQAQKLIHYTPAYFHHVPGMELSEKLAKIAP
GNSPKMVSFGNSGSDANDAIIKFARAYTGRQYIVSYMGSYHGSTYGSQTL
SGSSLNMTRKIGPMLPSVVHVPYPDSYRTYPGETEHDVSLRYFNEFKKPF
ESFLPADETACVLIEPIQGDGGIIKAPEEYMQLVYKFCHEHGILFAIDEV
NQGLGRTGKMWAIQQFKDIEPDLMSVGKSLASGMPLSAVIGKKEVMQSLD
APAHLFTTAGNPVCSAASLATLDVIEYEGLVEKSATDGAYAKQRFLEMQQ
RHPMIGDVRMWGLNGGIELVKDPKTKEPDSDAATKVIYYAFAHGVVIITL
AGNILRFQPPLVIPREQLDQALQVLDDAFTAVENGEVTI
3D structure
PDB5wya Crystal structure of the novel amino-acid racemase isoleucine 2-epimerase from Lactobacillus buchneri.
ChainA
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A22 Y142 E217 D250 N253 K280 T309 R408
Catalytic site (residue number reindexed from 1) A20 Y140 E215 D248 N251 K278 T307 R406
Enzyme Commision number 5.1.1.21: isoleucine 2-epimerase.
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 7VO A A54 S114 G115 S116 Y142 H143 E217 D250 V252 N253 K280 R408 A52 S112 G113 S114 Y140 H141 E215 D248 V250 N251 K278 R406
BS02 7VO A Y84 F308 T309 Y82 F306 T307
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0016853 isomerase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding

View graph for
Molecular Function
External links
PDB RCSB:5wya, PDBe:5wya, PDBj:5wya
PDBsum5wya
PubMed28471367
UniProtM1GRN3|ILE2E_LENBU Isoleucine 2-epimerase

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