Research workbench
The structure of muts bound to one molecule of ATP and one molecule of ADP
Analyse The structure of muts bound to one molecule of ATP and one molecule of ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OU4
- Type
- protein
- Length
- 1,389 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA mismatch repair protein muts
- UniProt
- P23909
- Ligands
- ATP, ADP, MG
- Pockets
- 14 · best druggability 0.84
Structure
electron microscopy · 2 distinct chains · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA mismatch repair protein muts | protein | 704 | 47% helix, 18% strand | P23909 |
| B | DNA mismatch repair protein muts | protein | 685 | 48% helix, 16% strand | P23909 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A, B
- ADP · Adenosine-5'-diphosphate · ligand · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 796 | 0.84 | 0.87 | 112 | MG, ADP |
| 2 | 826 | 0.80 | 0.83 | 75 | empty |
| 3 | 384 | 0.80 | 0.89 | 58 | MG, ATP |
| 4 | 642 | 0.78 | 0.84 | 80 | empty |
| 5 | 568 | 0.75 | 0.82 | 62 | empty |
Interfaces
1 interface between chains.
- A–B · 3448 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 7OU4 · The structure of MutS bound to one molecule of ATP and one molecule of ADP · the same entry in another collection · chain B against B, TM-score 1.00
- P23909 · AlphaFold monomer V2.0 prediction for DNA mismatch repair protein muts (P23909) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P23909
- Elsewhere: RCSB PDB 7OU4 · PDBe 7OU4 · UniProt P23909
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