Structure of PDB 5x7n Chain A

Receptor sequence
>5x7nA (length=442) Species: 196627 (Corynebacterium glutamicum ATCC 13032) [Search protein sequence]
TVENFNELPAHVWPRNAVRQEDGVVTVAGVPLPDLAEEYGTPLFVVDEDD
FRSRCRDMATAFGGPGNVHYASKAFLTKTIARWVDEEGLALDIASINELG
IALAAGFPASRITAHGNNKGVEFLRALVQNGVGHVVLDSAQELELLDYVA
AGEGKIQDVLIRVKPGIEAHTHEFIATSHEDQKFGFSLASGSAFEAAKAA
NNAENLNLVGLHCHVGSQVFDAEGFKLAAERVLGLYSQIHSELGVALPEL
DLGGGYGIAYTAAEEPLNVAEVASDLLTAVGKMAAELGIDAPTVLVEPGR
AIAGPSTVTIYEVGTTKDVHVDDDKTRRYIAVDGGMSDNIRPALYGSEYD
ARVVSRFAEGDPVSTRIVGSHCESGDILINDEIYPSDITSGDFLALAATG
AYCYAMSSRYNAFTRPAVVSVRAGSSRLMLRRETLDDILSLE
3D structure
PDB5x7n Structural basis for substrate specificity of meso-diaminopimelic acid decarboxylase from Corynebacterium glutamicum.
ChainA
Resolution1.72 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.20: diaminopimelate decarboxylase.
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 K75 H117 H216 G256 G257 E299 G301 R302 Y404 K73 H115 H214 G254 G255 E297 G299 R300 Y402
BS02 LYS A K75 R343 Y347 Y404 M408 K73 R341 Y345 Y402 M406
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008836 diaminopimelate decarboxylase activity
GO:0016830 carbon-carbon lyase activity
GO:0016831 carboxy-lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009085 lysine biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate

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Molecular Function
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Biological Process
External links
PDB RCSB:5x7n, PDBe:5x7n, PDBj:5x7n
PDBsum5x7n
PubMed29233695
UniProtP09890|DCDA_CORGL Diaminopimelate decarboxylase (Gene Name=lysA)

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