MolNFT v1 · #84550 · protein
Wild-type chorismate mutase of bacillus subtilis at 1.6 a resolution
3ZO8 · Chorismate mutase aroh: “Wild-type chorismate mutase of bacillus subtilis at 1.6 a resolution”. X-ray diffraction, 10 pockets (best druggability 0.80). MolNFT v1 #84550 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3ZO8
- Type
- protein
- Length
- 702 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate mutase aroh
- EC
- 5.4.99.5
- UniProt
- P19080
- Pockets
- 10 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Chorismate mutase aroh (EC 5.4.99.5) | protein | 117 | 32% helix, 30% strand | P19080 |
Pockets
10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 613 | 0.80 | 0.85 | 70 | empty |
| 2 | 315 | 0.66 | 0.81 | 28 | empty |
| 3 | 296 | 0.61 | 0.79 | 25 | empty |
| 4 | 350 | 0.60 | 0.77 | 34 | empty |
| 5 | 221 | 0.57 | 0.79 | 30 | empty |
Interfaces
12 interfaces between chains.
- D–E · 1098 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1079 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 1053 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 1047 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 1043 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3ZO8 · Wild-type chorismate mutase of Bacillus subtilis at 1.6 A resolution · the same entry in another collection · chain F against F, TM-score 1.00
- P19080 · AlphaFold monomer V2.0 prediction for chorismate mutase aroh (P19080) · a predicted model of the same protein · chain D 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 P19080
- Elsewhere: RCSB PDB 3ZO8 · PDBe 3ZO8 · UniProt P19080
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