MolNFT v1 · #119921 · protein
Crystal structure of lysine decarboxylase from selenomonas ruminantium in P43212 space group
5GJN · LYSINE/ORNITHINE decarboxylase: “Crystal structure of lysine decarboxylase from selenomonas ruminantium in P43212 space group”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.49). MolNFT v1 #119921 on GenesisL1: 3D…
- PDB
- 5GJN
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LYSINE/ORNITHINE decarboxylase
- EC
- 4.1.1.18
- UniProt
- O50657
- Ligands
- MG
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LYSINE/ORNITHINE decarboxylase (EC 4.1.1.18) | protein | 369 | 38% helix, 22% strand | O50657 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- 1PE · Pentaethylene glycol · additive · chains A
- PGE · Triethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 214 | 0.49 | 0.75 | 32 | GOL, MG |
| 2 | 66 | 0.31 | 0.74 | 13 | empty |
Compared structures
- 5GJN · Crystal structure of Lysine decarboxylase from Selenomonas ruminantium in P43212 space… · the same entry in another collection · chain A against A, TM-score 1.00
- O50657 · AlphaFold monomer V2.0 prediction for LYSINE/ORNITHINE decarboxylase (O50657) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O50657
- Elsewhere: RCSB PDB 5GJN · PDBe 5GJN · UniProt O50657
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