MolNFT v2 · #120229 · protein
Crystal structure of Lysine decarboxylase from Selenomonas ruminantium in P43212 space group
5GJN: “Crystal structure of Lysine decarboxylase from Selenomonas ruminantium in P43212 space group”. X-ray diffraction at 2, 1 ligand (MG). MolNFT v2 #120229 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5GJN
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Selenomonas ruminantium
- UniProt
- O50657
- Ligands
- MG
Structure
x-ray diffraction · resolution 2 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 369 | — | 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.
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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