Research workbench
Crystal structure of the chloroplast chorismate mutase from zea mays
Analyse Crystal structure of the chloroplast chorismate mutase from zea mays in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HJW
- Type
- protein
- Length
- 485 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate mutase
- EC
- 5.4.99.5
- UniProt
- B4FNK8
- Ligands
- TYR
- Pockets
- 6 · best druggability 0.89
Structure
x-ray diffraction · 2 distinct chains · 64% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chorismate mutase (EC 5.4.99.5) | protein | 240 | 64% helix, 2% strand | B4FNK8 |
| B | Chorismate mutase (EC 5.4.99.5) | protein | 245 | 64% helix, 1% strand | B4FNK8 |
Ligands and binding sites
- TYR · Tyrosine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 981 | 0.89 | 0.90 | 86 | TYR |
| 2 | 232 | 0.60 | 0.80 | 27 | empty |
| 3 | 187 | 0.56 | 0.80 | 23 | empty |
| 4 | 86 | 0.55 | 0.85 | 23 | empty |
| 5 | 135 | 0.46 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1994 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 6HJW · Crystal structure of the chloroplast chorismate mutase from Zea mays · the same entry in another collection · chain B against B, TM-score 1.00
- B4FNK8 · AlphaFold monomer V2.0 prediction for chorismate mutase 1, chloroplastic (B4FNK8) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 B4FNK8
- Elsewhere: RCSB PDB 6HJW · PDBe 6HJW · UniProt B4FNK8
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