Research workbench
Mismatch repair protein
Analyse Mismatch repair protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YK4
- Type
- protein
- Length
- 1,538 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA mismatch repair protein muts
- UniProt
- Q5F5J4
- Ligands
- ADP
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA mismatch repair protein muts | protein | 771 | 42% helix, 19% strand | Q5F5J4 |
| B | DNA mismatch repair protein muts | protein | 767 | 35% helix, 16% strand | Q5F5J4 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.72 | 0.91 | 30 | empty |
| 2 | 789 | 0.71 | 0.77 | 71 | empty |
| 3 | 202 | 0.71 | 0.88 | 42 | empty |
| 4 | 683 | 0.70 | 0.78 | 73 | empty |
| 5 | 343 | 0.69 | 0.82 | 57 | empty |
Interfaces
1 interface between chains.
- A–B · 1912 Ų buried · 15 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 Q5F5J4
- Elsewhere: RCSB PDB 5YK4 · PDBe 5YK4 · UniProt Q5F5J4
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