MolNFT v1 · #33346 · protein
Crystal structures of the monofunctional chorismate mutase from bacillus subtilis and its complex with a transition state analog
2CHS: “Crystal structures of the monofunctional chorismate mutase from bacillus subtilis and its complex with a…”. X-ray diffraction, 15 pockets (best druggability 0.59). MolNFT v1 #33346 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2CHS
- Type
- protein
- Length
- 1,368 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate mutase
- EC
- 5.4.99.5
- UniProt
- P19080
- Pockets
- 15 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Chorismate mutase (EC 5.4.99.5) | protein | 114 | 31% helix, 29% strand | P19080 |
Pockets
15 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 289 | 0.59 | 0.78 | 31 | empty |
| 2 | 299 | 0.59 | 0.78 | 26 | empty |
| 3 | 277 | 0.58 | 0.77 | 24 | empty |
| 4 | 282 | 0.57 | 0.77 | 27 | empty |
| 5 | 275 | 0.57 | 0.77 | 30 | empty |
Interfaces
15 interfaces between chains.
- A–C · 1053 Ų buried · 13 hydrogen bonds · protein-protein
- D–F · 1041 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 1041 Ų buried · 15 hydrogen bonds · protein-protein
- G–H · 1033 Ų buried · 13 hydrogen bonds · protein-protein
- J–K · 1032 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 2CHS · Crystal structures of the monofunctional chorismate mutase from bacillus subtilis and its… · the same entry in another collection · chain L against L, TM-score 1.00
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 2CHS · PDBe 2CHS · UniProt P19080
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