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Crystal structure of yeast IRC4
Analyse Crystal structure of yeast IRC4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5COG
- Type
- protein
- Length
- 337 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IRC4
- UniProt
- Q03036
- Ligands
- K, PO4, CL
- Pockets
- 3 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | IRC4 | protein | 168 | 70% helix, 1% strand | Q03036 |
| B | IRC4 | protein | 169 | 68% helix, 1% strand | Q03036 |
Ligands and binding sites
- K · Potassium ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.37 | 0.74 | 19 | empty |
| 2 | 70 | 0.34 | 0.75 | 17 | empty |
| 3 | 51 | 0.30 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 169 Ų buried · 3 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 Q03036
- Elsewhere: RCSB PDB 5COG · PDBe 5COG · UniProt Q03036
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