Research workbench
Crystal structure of the MATA1/MATALPHA2-3A heterodimer bound to DNA complex
Analyse Crystal structure of the MATA1/MATALPHA2-3A heterodimer bound to DNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LE8
- Type
- protein + DNA
- Length
- 167 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-D(*AP*CP*AP*TP*GP*TP*AP*AP*AP*AP*AP*TP*TP*TP*AP*CP*AP*TP *CP*A)-3'…
- UniProt
- P01366, Q6B184
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 4 distinct chains · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | 5'-D(*AP*CP*AP*TP*GP*TP*AP*AP*AP*AP*AP*TP*TP*TP*AP*CP*AP*TP *CP*A)-3' | dna | 20 | — | — |
| D | 5'-D(*TP*TP*GP*AP*TP*GP*TP*AP*AP*AP*TP*TP*TP*TP*TP*AP*CP*AP *TP*G)-3' | dna | 20 | — | — |
| A | Mating-type protein a-1 | protein | 53 | 68% helix, 0% strand | P01366 |
| B | Mating-type protein alpha-2 | protein | 74 | 58% helix, 0% strand | Q6B184 |
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 | 471 | 0.63 | 0.77 | 44 | empty |
| 2 | 118 | 0.45 | 0.78 | 17 | empty |
Interfaces
6 interfaces between chains.
- C–D · 847 Ų buried · 69 hydrogen bonds · nucleic-nucleic
- A–B · 667 Ų buried · 6 hydrogen bonds · protein-protein
- D–B · 440 Ų buried · 7 hydrogen bonds · protein-nucleic
- C–A · 401 Ų buried · 5 hydrogen bonds · protein-nucleic
- C–B · 349 Ų buried · 5 hydrogen bonds · protein-nucleic
Compared structures
- 1LE8 · Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex · the same entry in another collection · chain C against C, 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
- Every structure of UniProt P01366
- Every structure of UniProt Q6B184
- Elsewhere: RCSB PDB 1LE8 · PDBe 1LE8 · UniProt P01366 · UniProt Q6B184
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