Research workbench
Crystal structure of the chromoprotein eforred
Analyse Crystal structure of the chromoprotein eforred in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SWT
- Type
- protein
- Length
- 878 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chromoprotein eforred
- Ligands
- NRQ
- Pockets
- 10 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chromoprotein eforred | protein | 221 | 5% helix, 56% strand | — |
| B, C, D | Chromoprotein eforred | protein | 219 | 5% helix, 57% strand | — |
Ligands and binding sites
- NRQ · {(4Z)-4-(4-hydroxybenzylidene)-2-[3-(methylthio) propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1131 | 0.83 | 0.84 | 108 | empty |
| 2 | 101 | 0.78 | 0.98 | 29 | NRQ |
| 3 | 99 | 0.76 | 0.97 | 29 | NRQ |
| 4 | 90 | 0.76 | 0.98 | 29 | NRQ |
| 5 | 69 | 0.73 | 0.97 | 20 | NRQ |
Interfaces
6 interfaces between chains.
- A–C · 1475 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 1449 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 1086 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1053 Ų buried · 19 hydrogen bonds · protein-protein
- A–D · 29 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 cofactor (chromophore).
Compared structures
- 7SWT · Crystal structure of the chromoprotein eforRED · the same entry in another collection · chain A against A, 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
- Elsewhere: RCSB PDB 7SWT · PDBe 7SWT
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