MolNFT v1 · #63938 · protein
Crystal structure of N-acetylglucosamine-1-phosphate uridyltransferase (glmu) from mycobacterium tuberculosis in a cubic space group.
3FOQ · Bifunctional protein glmu: “Crystal structure of N-acetylglucosamine-1-phosphate uridyltransferase (glmu) from mycobacterium tuberculosis…”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.64). MolNFT v1 #63938 on…
- PDB
- 3FOQ
- Type
- protein
- Length
- 439 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
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein glmu (EC 2.7.7.23, 2.3.1.157) | protein | 439 | 21% helix, 30% strand | P96382 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 496 | 0.64 | 0.76 | 45 | empty |
| 2 | 127 | 0.41 | 0.75 | 21 | empty |
Compared structures
- 3FOQ · Crystal structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from… · 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 3FOQ · PDBe 3FOQ · UniProt P96382
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