Research workbench
Crystal structure of glmu from mycobacterium tuberculosis, ligand-free form
Analyse Crystal structure of glmu from mycobacterium tuberculosis, ligand-free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D98
- Type
- protein
- Length
- 390 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional protein glmu
- EC
- 2.7.7.23, 2.3.1.157
- UniProt
- P96382
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein glmu (EC 2.7.7.23, 2.3.1.157) | protein | 390 | 26% helix, 31% strand | P96382 |
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 | 636 | 0.77 | 0.82 | 57 | empty |
| 2 | 89 | 0.36 | 0.75 | 15 | empty |
| 3 | 72 | 0.35 | 0.76 | 14 | empty |
Compared structures
- 3D98 · Crystal structure of GlmU from Mycobacterium tuberculosis, ligand-free form · 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 P96382
- Elsewhere: RCSB PDB 3D98 · PDBe 3D98 · UniProt P96382
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.