MolNFT v1 · #104111 · protein
Crystal structure of acinetobacter sp. DL28 L-ribose isomerase mutant E204Q in complex with L-ribulose
4Q0V: “Crystal structure of acinetobacter sp. DL28 L-ribose isomerase mutant E204Q in complex with L-ribulose”. X-ray diffraction, 4 ligands (RUU, QDK, NCO), 3 pockets (best druggability 0.62). MolNFT v1 #104111 on GenesisL1: 3D structure…
- PDB
- 4Q0V
- Type
- protein
- Length
- 249 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-ribose isomerase
- EC
- 5.3.1.-
- UniProt
- Q93UQ5
- Ligands
- RUU, QDK, NCO, CO
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-ribose isomerase (EC 5.3.1.-) | protein | 249 | 20% helix, 27% strand | Q93UQ5 |
Ligands and binding sites
- RUU · alpha-L-ribulofuranose · ligand · 5 copies · chains A
- QDK · L-ribulose · ligand · 2 copies · chains A
- NCO · Cobalt hexammine(iii) · ligand · chains A
- CO · Cobalt (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.62 | 0.81 | 38 | RUU, QDK |
| 2 | 95 | 0.34 | 0.74 | 17 | empty |
| 3 | 52 | 0.29 | 0.75 | 14 | empty |
Compared structures
- 4Q0V · Crystal structure of Acinetobacter sp. DL28 L-ribose isomerase mutant E204Q in complex… · 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 Q93UQ5
- Elsewhere: RCSB PDB 4Q0V · PDBe 4Q0V · UniProt Q93UQ5
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