MolNFT v1 · #50534 · protein
Crystal structure of udp-N-acetylglucosamine enolpyruvyl transferase from haemophilus influenzae in complex with udp-N-acetylglucosamine and fosfomycin
2RL2 · Udp-N-acetylglucosamine 1- carboxyvinyltransferase: “Crystal structure of udp-N-acetylglucosamine enolpyruvyl transferase from haemophilus influenzae in complex…”. X-ray diffraction, 3 ligands (GG6, UD1, SO4), 2 pockets (best…
- PDB
- 2RL2
- Type
- protein
- Length
- 420 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine 1- carboxyvinyltransferase
- EC
- 2.5.1.7
- UniProt
- P45025
- Ligands
- GG6, UD1, SO4
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1- carboxyvinyltransferase (EC 2.5.1.7) | protein | 420 | 35% helix, 27% strand | P45025 |
Ligands and binding sites
- GG6 · [(1S,2S)-1,2-dihydroxypropyl]phosphonic acid · ligand · chains A
- UD1 · Uridine-diphosphate-N-acetylglucosamine · ligand · chains A
- SO4 · Sulfate ion · ion · 3 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 | 637 | 0.78 | 0.84 | 61 | SO4, GG6, UD1 |
| 2 | 58 | 0.33 | 0.77 | 17 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2RL2 · Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus… · the same entry in another collection · chain A against A, TM-score 1.00
- P45025 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase… · 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 P45025
- Elsewhere: RCSB PDB 2RL2 · PDBe 2RL2 · UniProt P45025
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