Research workbench
Crystal structure of uncharacterised protein COCH_1243 from capnocytophaga ochracea dsm 7271
Analyse Crystal structure of uncharacterised protein COCH_1243 from capnocytophaga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4W9R
- Type
- protein
- Length
- 721 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- C7M590
- Pockets
- 4 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 360 | 52% helix, 19% strand | C7M590 |
| B | Uncharacterized protein | protein | 361 | 51% helix, 19% strand | C7M590 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A, B
- ACT · Acetate ion · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.54 | 0.78 | 30 | empty |
| 2 | 163 | 0.40 | 0.73 | 27 | GOL |
| 3 | 145 | 0.38 | 0.73 | 24 | ACT |
| 4 | 81 | 0.34 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1283 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 4W9R · Crystal structure of uncharacterised protein Coch_1243 from Capnocytophaga ochracea DSM… · 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
- Every structure of UniProt C7M590
- Elsewhere: RCSB PDB 4W9R · PDBe 4W9R · UniProt C7M590
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