Structure of PDB 5wya Chain C

Receptor sequence
>5wyaC (length=440) Species: 1581 (Lentilactobacillus buchneri) [Search protein sequence]
GKLDKASKLIDEENKYYARSARINYYNLVIDHAHGATLVDVDGNKYIDLL
ASASAINVGHTHEKVVKAIADQAQKLIHYTPAYFHHVPGMELSEKLAKIA
PGNSPKMVSFGNSGSDANDAIIKFARAYTGRQYIVSYMGSYHGSTYGSQT
LSGSSLNMTRKIGPMLPSVVHVPYPDSYRTYPGETEHDVSLRYFNEFKKP
FESFLPADETACVLIEPIQGDGGIIKAPEEYMQLVYKFCHEHGILFAIDE
VNQGLGRTGKMWAIQQFKDIEPDLMSVGKSLASGMPLSAVIGKKEVMQSL
DAPAHLFTTAGNPVCSAASLATLDVIEYEGLVEKSATDGAYAKQRFLEMQ
QRHPMIGDVRMWGLNGGIELVKDPKTKEPDSDAATKVIYYAFAHGVVIIT
LAGNILRFQPPLVIPREQLDQALQVLDDAFTAVENGEVTI
3D structure
PDB5wya Crystal structure of the novel amino-acid racemase isoleucine 2-epimerase from Lactobacillus buchneri.
ChainC
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) A21 Y141 E216 D249 N252 K279 T308 R407
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 C A54 G115 S116 Y142 H143 D250 V252 N253 K280 R408 A53 G114 S115 Y141 H142 D249 V251 N252 K279 R407
BS02 7VO C Y84 F308 T309 Y83 F307 T308
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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