Research workbench
E. COLI lpxh- 8 mutations
Analyse E. COLI lpxh- 8 mutations in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WLY
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-2,3-diacylglucosamine hydrolase
- EC
- 3.6.1.54
- UniProt
- Q0P6L0
- Ligands
- MN, CL
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-2,3-diacylglucosamine hydrolase (EC 3.6.1.54) | protein | 220 | 33% helix, 26% strand | Q0P6L0 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- FMT · Formic acid · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.30 | 0.74 | 15 | CL |
Compared structures
- 5WLY · E. coli LpxH- 8 mutations · 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 Q0P6L0
- Elsewhere: RCSB PDB 5WLY · PDBe 5WLY · UniProt Q0P6L0
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