Structure of PDB 5gjp Chain A

Receptor sequence

>5gjpA (length=381) Species: 971 (Selenomonas ruminantium)

MKNFRLSEKEVKTLAKRIPTPFLVASLDKVEENYQFMRRHLPRAGVFYAM
KANPTPEILSLLAGLGSHFDVASAGEMEILHELGVDGSQMIYANPVKDAR
GLKAAADYNVRRFTFDDPSEIDKMAKAVPGADVLVRIAVRNTKFGAPVEE
ALDLLKAAQDAGLHAMGICFHVGSQSLSTAAYEEALLVARRLFDEAEEMG
MHLTDLDIGGGFPVPDAKGLNVDLAAMMEAINKQIDRLFPDTAVWTEPGR
YMCGTAVNLVTSVIGTKTRGEQPWYILDEGIYGCFSGIMYDHWTYPLHCF
GKGNKKPSTFGGPSCDGIDVLYRDFMAPELKIGDKVLVTEMGSYTSVSAT
RFNGFYLAPTIIFEDQPEYAARLTEDDDVKK

3D structure

• PDB: 5gjp Crystal Structure and Pyridoxal 5-Phosphate Binding Property of Lysine Decarboxylase from Selenomonas ruminantium
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K51 H179 E255
• Catalytic site (residue number reindexed from 1): K51 H171 E247
• Enzyme Commision number: 4.1.1.17: ornithine decarboxylase.
  4.1.1.18: lysine 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	N2P	A	Y298 D299 Y352	Y290 D291 Y344
BS02	PLP	A	A49 K51 H179 S182 G219 E255 G257 R258 Y352	A49 K51 H171 S174 G211 E247 G249 R250 Y344

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004586 ornithine decarboxylase activity
• GO:0008923 lysine decarboxylase activity
• GO:0016831 carboxy-lyase activity

Biological Process

• GO:0006596 polyamine biosynthetic process
• GO:0008295 spermidine biosynthetic process
• GO:0009446 putrescine biosynthetic process
• GO:0033387 putrescine biosynthetic process from ornithine

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:5gjp, PDBe:5gjp, PDBj:5gjp
• PDBsum: 5gjp
• PubMed: 27861532
• UniProt: O50657|DCLO_SELRU Lysine/ornithine decarboxylase (Gene Name=ldc)