Research workbench
Crystal structure of the unbound nuclease domain of COLE7
Analyse Crystal structure of the unbound nuclease domain of COLE7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1M08
- Type
- protein
- Length
- 262 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Colicin E7
- EC
- 3.1.-.-
- UniProt
- Q47112
- Ligands
- ZN, PO4
- Pockets
- 4 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Colicin E7 (EC 3.1.-.-) | protein | 131 | 38% helix, 17% strand | Q47112 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.39 | 0.76 | 26 | PO4 |
| 2 | 91 | 0.38 | 0.76 | 22 | ZN, PO4 |
| 3 | 94 | 0.36 | 0.75 | 18 | empty |
| 4 | 87 | 0.34 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 574 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
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 Q47112
- Elsewhere: RCSB PDB 1M08 · PDBe 1M08 · UniProt Q47112
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