Research workbench
Crystal structure of MTA1-P1-P2 complex
Analyse Crystal structure of MTA1-P1-P2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F4L
- Type
- protein
- Length
- 752 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transmembrane protein, putative; Mt-A70 family protein; P1 protein
- UniProt
- I7M8B9, Q22GC0, Q22VV9
- Pockets
- 7 · best druggability 0.59
Structure
x-ray diffraction · 6 distinct chains · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Transmembrane protein, putative | protein | 130 | 55% helix, 5% strand | I7M8B9 |
| C | Mt-A70 family protein | protein | 215 | 36% helix, 21% strand | Q22GC0 |
| D | Mt-A70 family protein | protein | 216 | 34% helix, 20% strand | Q22GC0 |
| E | P1 protein | protein | 37 | 68% helix, 0% strand | Q22VV9 |
| F | P1 protein | protein | 25 | 84% helix, 0% strand | Q22VV9 |
| A | Transmembrane protein, putative | protein | 129 | 56% helix, 5% strand | I7M8B9 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 185 | 0.59 | 0.81 | 31 | empty |
| 2 | 202 | 0.53 | 0.78 | 34 | empty |
| 3 | 95 | 0.48 | 0.82 | 27 | empty |
| 4 | 189 | 0.48 | 0.76 | 22 | empty |
| 5 | 94 | 0.39 | 0.76 | 15 | empty |
Interfaces
7 interfaces between chains.
- B–C · 1772 Ų buried · 16 hydrogen bonds · protein-protein
- D–A · 1718 Ų buried · 15 hydrogen bonds · protein-protein
- D–E · 1084 Ų buried · 9 hydrogen bonds · protein-protein
- C–F · 805 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 759 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 19 modified (engineered).
Compared structures
- 7F4L · Crystal structure of MTA1-p1-p2 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
- Every structure of UniProt I7M8B9
- Every structure of UniProt Q22GC0
- Every structure of UniProt Q22VV9
- Elsewhere: RCSB PDB 7F4L · PDBe 7F4L · UniProt I7M8B9 · UniProt Q22GC0 · UniProt Q22VV9
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