MolNFT v1 · #90411 · protein
Unliganded E. cloacae R91K mura
4EII · Udp-N-acetylglucosamine 1-carboxyvinyltransferase: “Unliganded E. cloacae R91K mura”. X-ray diffraction, 2 pockets (best druggability 0.68). MolNFT v1 #90411 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4EII
- Type
- protein
- Length
- 419 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
- P33038
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) | protein | 419 | 34% helix, 27% strand | P33038 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- PGE · Triethylene glycol · 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 | 697 | 0.68 | 0.76 | 53 | EDO |
| 2 | 77 | 0.39 | 0.78 | 17 | empty |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
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 P33038
- Elsewhere: RCSB PDB 4EII · PDBe 4EII · UniProt P33038
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