Research workbench
E.coli MutS R697A: an ATPase-asymmetry mutant
Analyse E.coli MutS R697A: an ATPase-asymmetry mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NG9
- Type
- protein + DNA
- Length
- 1,595 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Escherichia coli; SYNTHETIC CONSTRUCT
- Molecule
- 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP*CP*AP*CP*CP*AP*GP*TP*GP*TP*CP*AP*GP*CP*GP*TP*CP*CP*TP*…
- UniProt
- P23909
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · resolution 2.6 · 4 distinct chains · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP*CP*AP*CP*CP*AP*GP*TP*GP*TP*CP*AP*GP*CP*GP*TP*CP*CP*TP*AP*T)-3' | dna | 18 | — | — |
| F | 5'-D(*AP*TP*AP*GP*GP*AP*CP*GP*CP*TP*GP*AP*CP*AP*CP*TP*GP*GP*TP*GP*CP*TP*TP*GP*GP*CP*AP*GP*CP*T)-3' | dna | 17 | — | — |
| A | DNA mismatch repair protein MutS | protein | 794 | 45% helix, 18% strand | P23909 |
| B | DNA mismatch repair protein MutS | protein | 766 | 48% helix, 18% strand | P23909 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · 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
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 833 | 0.75 | 0.79 | 82 | empty |
| 2 | 922 | 0.74 | 0.78 | 85 | MG, ADP |
| 3 | 344 | 0.69 | 0.83 | 44 | empty |
| 4 | 294 | 0.69 | 0.84 | 31 | empty |
| 5 | 476 | 0.64 | 0.77 | 38 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2814 Ų buried · 40 hydrogen bonds · protein-protein
- E–F · 823 Ų buried · 81 hydrogen bonds · nucleic-nucleic
- F–A · 654 Ų buried · 11 hydrogen bonds · protein-nucleic
- E–A · 647 Ų buried · 12 hydrogen bonds · protein-nucleic
- E–B · 394 Ų buried · 5 hydrogen bonds · protein-nucleic
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 P23909
- Elsewhere: RCSB PDB 1NG9 · PDBe 1NG9 · UniProt P23909
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