Structure of PDB 3co8 Chain B

Receptor sequence
>3co8B (length=345) Species: 203123 (Oenococcus oeni PSU-1) [Search protein sequence]
RSTRIEFSKSSLAYNVQYTKQVSGAKTLWLAVKSNAYGHGLLQVSKIARE
CGVDGLAVSVLDEGIAIRQAGIDDFILILGPIDVKYAPIASKYHFLTTVS
SLDWLKSADKILGKEKLSVNLAVDTGMNRIGVRSKKDLKDEIEFLQEHSD
HFSYDGIFTHFASSDNPDDHYFQRQKNRWYELIDGLIMPRYVHVMNSGAA
MYHSKELPGCNSIARVGTVVYGVEPSEGVLGPIDKLKPVFELKSALTFVK
KWIGTLPIGYGDGWLAEYQDFQLLIDGQKCRQVGQIAMDQMMVALPHEYP
IGTEVTLIGKSGKYENTLYDLHKHSGVPPWKITVAFSDRLKRMVV
3D structure
PDB3co8 Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5'-phosphate.
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K39 R135 H166 R221 A312 D314
Catalytic site (residue number reindexed from 1) K33 R129 H160 R215 A287 D289
Enzyme Commision number 5.1.1.5: lysine 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 PLP B K39 Y43 L85 R135 H166 S203 R221 G223 T224 K33 Y37 L79 R129 H160 S197 R215 G217 T218
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008784 alanine racemase activity
GO:0016853 isomerase activity
GO:0018113 lysine racemase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006522 alanine metabolic process
GO:0009252 peptidoglycan biosynthetic process
GO:0030632 D-alanine biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3co8, PDBe:3co8, PDBj:3co8
PDBsum3co8
PubMed23295479
UniProtQ04HB7|LYSR_OENOB Lysine racemase (Gene Name=OEOE_0162)

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