Structure of PDB 4ysn Chain C

Receptor sequence
>4ysnC (length=448) Species: 1581 (Lentilactobacillus buchneri) [Search protein sequence]
EGRHMELMGKLDKASKLIDEENKYYARSARINYYNLVIDHAHGATLVDVD
GNKYIDLLASASAINVGHTHEKVVKAIADQAQKLIHYTPAYFHHVPGMEL
SEKLAKIAPGNSPKMVSFGNSGSDANDAIIKFARAYTGRQYIVSYMGSYH
GSTYGSQTLSGSSLNMTRKIGPMLPSVVHVPYPDSYRTYPGETEHDVSLR
YFNEFKKPFESFLPADETACVLIEPIQGDGGIIKAPEEYMQLVYKFCHEH
GILFAIDEVNQGLGRTGKMWAIQQFKDIEPDLMSVGKSLASGMPLSAVIG
KKEVMQSLDAPAHLFTTAGNPVCSAASLATLDVIEYEGLVEKSATDGAYA
KQRFLEMQQRHPMIGDVRMWGLNGGIELVKDPKTKEPDSDAATKVIYYAF
AHGVVIITLAGNILRFQPPLVIPREQLDQALQVLDDAFTAVENGEVTI
3D structure
PDB4ysn Crystal structure of the novel amino-acid racemase isoleucine 2-epimerase from Lactobacillus buchneri.
ChainC
Resolution1.94 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) A29 Y149 E224 D257 N260 K287 T316 R415
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 C S114 G115 S116 Y142 H143 E217 D250 V252 K280 S121 G122 S123 Y149 H150 E224 D257 V259 K287
BS02 PLP C F308 T309 F315 T316
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:4ysn, PDBe:4ysn, PDBj:4ysn
PDBsum4ysn
PubMed28471367
UniProtM1GRN3|ILE2E_LENBU Isoleucine 2-epimerase

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