Research workbench
ARG90CIT chorismate mutase of bacillus subtilis at 1.6 a resolution
Analyse ARG90CIT chorismate mutase of bacillus subtilis at 1.6 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZOP
- Type
- protein
- Length
- 696 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
- Ligands
- CIR
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Chorismate mutase aroh (EC 5.4.99.5) | protein | 116 | 33% helix, 28% strand | P19080 |
Ligands and binding sites
- CIR · Citrulline · ligand · 6 copies · chains A, C, B, D, F, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 967 | 0.79 | 0.81 | 109 | CIR |
| 2 | 326 | 0.70 | 0.83 | 43 | CIR |
| 3 | 347 | 0.69 | 0.82 | 39 | CIR |
| 4 | 232 | 0.69 | 0.85 | 37 | CIR |
| 5 | 359 | 0.67 | 0.81 | 36 | CIR |
Interfaces
11 interfaces between chains.
- B–C · 1104 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 1059 Ų buried · 17 hydrogen bonds · protein-protein
- E–F · 1054 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1052 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 1048 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 covalent (covalent ligand).
Compared structures
- 3ZOP · Arg90Cit chorismate mutase of Bacillus subtilis at 1.6 A resolution · the same entry in another collection · chain E against E, TM-score 1.00
- P19080 · AlphaFold monomer V2.0 prediction for chorismate mutase aroh (P19080) · 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 P19080
- Elsewhere: RCSB PDB 3ZOP · PDBe 3ZOP · UniProt P19080
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