MolNFT v1 · #51203 · protein
Characterization of substrate binding and catalysis of the potential antibacterial target N-acetylglucosamine-1- phosphate uridyltransferase (glmu)
2V0I · Bifunctional protein glmu: “Characterization of substrate binding and catalysis of the potential antibacterial target…”. X-ray diffraction, 2 ligands (UD1, SO4), 2 pockets (best druggability 0.72). MolNFT v1 #51203 on GenesisL1: 3D…
- PDB
- 2V0I
- Type
- protein
- Length
- 450 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional protein glmu
- EC
- 2.-.-.-
- UniProt
- P43889
- Ligands
- UD1, SO4
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein glmu (EC 2.-.-.-) | protein | 450 | 21% helix, 34% strand | P43889 |
Ligands and binding sites
- UD1 · Uridine-diphosphate-N-acetylglucosamine · ligand · chains A
- SO4 · Sulfate ion · ion · 6 copies · chains A
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 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 | 577 | 0.72 | 0.80 | 46 | UD1, SO4 |
| 2 | 232 | 0.49 | 0.75 | 26 | empty |
Compared structures
- 2V0I · Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target… · the same entry in another collection · chain A against A, TM-score 1.00
- P43889 · AlphaFold monomer V2.0 prediction for bifunctional protein glmu (P43889) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P43889
- Elsewhere: RCSB PDB 2V0I · PDBe 2V0I · UniProt P43889
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