Research workbench
Crystal structure of N-acetylglucosamine 1-phosphate uridyltransferase
Analyse Crystal structure of N-acetylglucosamine 1-phosphate uridyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FXJ
- Type
- protein
- Length
- 651 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine pyrophosphorylase
- EC
- 2.7.7.23
- UniProt
- P0ACC7
- Ligands
- SO4
- Pockets
- 6 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) | protein | 327 | 29% helix, 30% strand | P0ACC7 |
| B | Udp-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) | protein | 324 | 30% helix, 30% strand | P0ACC7 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 636 | 0.68 | 0.77 | 55 | MES |
| 2 | 511 | 0.66 | 0.77 | 42 | empty |
| 3 | 119 | 0.52 | 0.81 | 21 | empty |
| 4 | 190 | 0.45 | 0.74 | 26 | empty |
| 5 | 133 | 0.41 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 313 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1FXJ · Crystal structure of N-acetylglucosamine 1-phosphate uridyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
- P0ACC7 · AlphaFold monomer V2.0 prediction for bifunctional protein glmu (P0ACC7) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P0ACC7
- Elsewhere: RCSB PDB 1FXJ · PDBe 1FXJ · UniProt P0ACC7
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