Research workbench
Structure of E. COLI glmu: analysis of pyrophosphorylase and acetyltransferase active sites
Analyse Structure of E. COLI glmu: analysis of pyrophosphorylase and acetyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HV9
- Type
- protein
- Length
- 899 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
- COA, UD1, CO
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) | protein | 449 | 20% helix, 34% strand | P0ACC7 |
| B | Udp-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) | protein | 450 | 20% helix, 33% strand | P0ACC7 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, B
- UD1 · Uridine-diphosphate-N-acetylglucosamine · ligand · 2 copies · chains A, B
- CO · Cobalt (II) ion · metal · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 491 | 0.74 | 0.83 | 41 | CO, UD1 |
| 2 | 504 | 0.66 | 0.78 | 49 | UD1 |
| 3 | 144 | 0.44 | 0.76 | 19 | empty |
| 4 | 144 | 0.40 | 0.74 | 24 | empty |
| 5 | 78 | 0.36 | 0.76 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 121 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1HV9 · Structure of E. COLI glmu: analysis of pyrophosphorylase and acetyltransferase active… · 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 A 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 1HV9 · PDBe 1HV9 · UniProt P0ACC7
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