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Crystal structure of taq muts
Analyse Crystal structure of taq muts in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EWR
- Type
- protein
- Length
- 976 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA mismatch repair protein muts
- UniProt
- Q56215
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA mismatch repair protein muts | protein | 447 | 44% helix, 16% strand | Q56215 |
| B | DNA mismatch repair protein muts | protein | 529 | 46% helix, 14% strand | Q56215 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 951 | 0.77 | 0.80 | 111 | empty |
| 2 | 107 | 0.65 | 0.89 | 30 | empty |
| 3 | 387 | 0.63 | 0.78 | 47 | empty |
| 4 | 372 | 0.61 | 0.77 | 37 | empty |
| 5 | 164 | 0.55 | 0.80 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 2025 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
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 Q56215
- Elsewhere: RCSB PDB 1EWR · PDBe 1EWR · UniProt Q56215
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