Research workbench
C-terminal domain of bacillus subtilis mutl crystal form I
Analyse C-terminal domain of bacillus subtilis mutl crystal form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GAB
- Type
- protein
- Length
- 736 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA mismatch repair protein mutl
- UniProt
- P49850
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 4 distinct chains · 44% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA mismatch repair protein mutl | protein | 183 | 45% helix, 25% strand | P49850 |
| B | DNA mismatch repair protein mutl | protein | 183 | 44% helix, 25% strand | P49850 |
| C | DNA mismatch repair protein mutl | protein | 184 | 44% helix, 26% strand | P49850 |
| D | DNA mismatch repair protein mutl | protein | 186 | 42% helix, 25% strand | P49850 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 393 | 0.62 | 0.77 | 47 | empty |
| 2 | 65 | 0.31 | 0.75 | 18 | empty |
Interfaces
2 interfaces between chains.
- B–C · 1041 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 256 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3GAB · C-terminal domain of Bacillus subtilis MutL crystal form I · the same entry in another collection · chain D against D, TM-score 1.00
- P49850 · AlphaFold monomer V2.0 prediction for DNA mismatch repair protein mutl (P49850) · a predicted model of the same protein · chain C against A, TM-score 0.95
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 P49850
- Elsewhere: RCSB PDB 3GAB · PDBe 3GAB · UniProt P49850
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