MolNFT v1 · #92676 · protein
2.7 ångström resolution structure of 3-phosphoshikimate 1- carboxyvinyltransferase (aroa) from coxiella burnetii in a second conformational state
4GFP · 3-phosphoshikimate 1-carboxyvinyltransferase: “2.7 ångström resolution structure of 3-phosphoshikimate 1- carboxyvinyltransferase (aroa) from coxiella…”. X-ray diffraction, 2 pockets (best druggability 0.80). MolNFT v1 #92676 on…
- PDB
- 4GFP
- Type
- protein
- Length
- 408 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-phosphoshikimate 1-carboxyvinyltransferase
- EC
- 2.5.1.19
- UniProt
- Q83E11
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) | protein | 408 | 35% helix, 26% strand | Q83E11 |
Ligands and binding sites
- BME · Beta-mercaptoethanol · additive · 2 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 | 984 | 0.80 | 0.82 | 99 | empty |
| 2 | 51 | 0.30 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 2 covalent, 1 disulfide (additive adduct, disulfide).
Compared structures
- 4GFP · 2.7 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA)… · the same entry in another collection · chain A against A, TM-score 1.00
- Q83E11 · AlphaFold monomer V2.0 prediction for 3-phosphoshikimate 1-carboxyvinyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q83E11
- Elsewhere: RCSB PDB 4GFP · PDBe 4GFP · UniProt Q83E11
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