Structure of PDB 5ll3 Chain A

Receptor sequence
>5ll3A (length=417) Species: 1581 (Lentilactobacillus buchneri) [Search protein sequence]
NYYNLVIDHAHGATLVDVDGNKYIDLLASASAINVGHTHEKVVKAIADQA
QKLIHYTPAYFHHVPGMELSEKLAKIAPGNSPKMVSFGNSGSDANDAIIK
FARAYTGRQYIVSYMGSYHGSTYGSQTLSGSSLNMTRKIGPMLPSVVHVP
YPDSYRTYPGETEHDVSLRYFNEFKKPFESFLPADETACVLIEPIQGDGG
IIKAPEEYMQLVYKFCHEHGILFAIDEVNQGLGRTGKMWAIQQFKDIEPD
LMSVGKSLASGMPLSAVIGKKEVMQSLDAPAHLFTTAGNPVCSAASLATL
DVIEYEGLVEKSATDGAYAKQRFLEMQQRHPMIGDVRMWGLNGGIELVKD
PKTKEPDSDAATKVIYYAFAHGVVIITLAGNILRFQPPLVIPREQLDQAL
QVLDDAFTAVENGEVTI
3D structure
PDB5ll3 Structural insights into the substrate recognition and reaction specificity of the PLP-dependent fold-type I isoleucine 2-epimerase from Lactobacillus buchneri.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y142 E217 D250 N253 K280 T309 R408
Catalytic site (residue number reindexed from 1) Y118 E193 D226 N229 K256 T285 R384
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 PLP A S114 G115 S116 Y142 H143 D250 V252 N253 K280 S90 G91 S92 Y118 H119 D226 V228 N229 K256
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:5ll3, PDBe:5ll3, PDBj:5ll3
PDBsum5ll3
PubMed28344038
UniProtM1GRN3|ILE2E_LENBU Isoleucine 2-epimerase

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