MolNFT v1 · #47089 · protein
Crystal structure of putative L-alanine-dl-glutamate epimerase from burkholderia xenovorans strain LB400
2OO6: “Crystal structure of putative L-alanine-dl-glutamate epimerase from burkholderia xenovorans strain LB400”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.72). MolNFT v1 #47089 on GenesisL1: 3D structure, binding…
- PDB
- 2OO6
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative L-alanine-dl-glutamate epimerase
- UniProt
- Q13PB7
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative L-alanine-dl-glutamate epimerase | protein | 393 | 40% helix, 19% strand | Q13PB7 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.72 | 0.90 | 28 | SO4 |
| 2 | 79 | 0.55 | 0.86 | 25 | empty |
| 3 | 111 | 0.47 | 0.79 | 17 | empty |
| 4 | 53 | 0.28 | 0.75 | 13 | empty |
Compared structures
- 2OO6 · Crystal structure of putative L-alanine-DL-glutamate epimerase from Burkholderia… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q13PB7
- Elsewhere: RCSB PDB 2OO6 · PDBe 2OO6 · UniProt Q13PB7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.