Research workbench
Mutm (fpg)-DNA estranged thymine mismatch recognition complex
Analyse Mutm (fpg)-DNA estranged thymine mismatch recognition complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L2C
- Type
- protein + DNA
- Length
- 283 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'- D(*AP*G*GP*TP*AP*GP*AP*CP*TP*TP*GP*GP*AP*CP*GP*C)-3'…
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | 5'- D(*AP*G*GP*TP*AP*GP*AP*CP*TP*TP*GP*GP*AP*CP*GP*C)-3' | dna | 12 | — | — |
| C | 5'-D(*TP*GP*C*GP*TP*CP*CP*AP*(HPD) P*GP*TP*CP*TP*AP*CP*C)-3' | dna | 12 | — | — |
| A | Mutm | protein | 259 | 31% helix, 25% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 593 | 0.67 | 0.77 | 44 | empty |
| 2 | 100 | 0.39 | 0.76 | 21 | empty |
Interfaces
3 interfaces between chains.
- C–A · 645 Ų buried · 13 hydrogen bonds · protein-nucleic
- B–C · 484 Ų buried · 49 hydrogen bonds · nucleic-nucleic
- B–A · 416 Ų buried · 5 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
- 1L2C · MutM (Fpg)-DNA Estranged Thymine Mismatch Recognition Complex · the same entry in another collection · chain B against B, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 1L2C · PDBe 1L2C
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