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Crystal structure of mad MH2 domain
Analyse Crystal structure of mad MH2 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DIT
- Type
- protein
- Length
- 560 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein mothers against dpp
- UniProt
- P42003
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein mothers against dpp | protein | 186 | 28% helix, 30% strand | P42003 |
| B | Protein mothers against dpp | protein | 186 | 28% helix, 32% strand | P42003 |
| C | Protein mothers against dpp | protein | 188 | 27% helix, 28% strand | P42003 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 530 | 0.65 | 0.76 | 35 | empty |
| 2 | 201 | 0.45 | 0.74 | 25 | empty |
| 3 | 126 | 0.42 | 0.75 | 33 | empty |
| 4 | 66 | 0.38 | 0.79 | 18 | empty |
| 5 | 61 | 0.38 | 0.79 | 17 | empty |
Interfaces
2 interfaces between chains.
- A–B · 288 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 232 Ų buried · 4 hydrogen bonds · protein-protein
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 P42003
- Elsewhere: RCSB PDB 3DIT · PDBe 3DIT · UniProt P42003
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