Research workbench
Crystal structure of MAD1-MAD2 reveals a conserved MAD2 binding motif in MAD1 and CDC20.
Analyse Crystal structure of MAD1-MAD2 reveals a conserved MAD2 binding motif in MAD1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GO4
- Type
- protein
- Length
- 1,146 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitotic spindle assembly checkpoint protein MAD2A; Mitotic spindle assembly checkpoint…
- UniProt
- Q13257, Q9Y6D9
- Pockets
- 15 · best druggability 0.77
Structure
x-ray diffraction · 6 distinct chains · 46% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitotic spindle assembly checkpoint protein MAD2A | protein | 196 | 35% helix, 33% strand | Q13257 |
| B, C | Mitotic spindle assembly checkpoint protein MAD2A | protein | 195 | 35% helix, 35% strand | Q13257 |
| D | Mitotic spindle assembly checkpoint protein MAD2A | protein | 193 | 34% helix, 34% strand | Q13257 |
| E, F | Mitotic spindle assembly checkpoint protein MAD1 | protein | 87 | 71% helix, 7% strand | Q9Y6D9 |
| G | Mitotic spindle assembly checkpoint protein MAD1 | protein | 100 | 71% helix, 8% strand | Q9Y6D9 |
| H | Mitotic spindle assembly checkpoint protein MAD1 | protein | 93 | 71% helix, 8% strand | Q9Y6D9 |
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 964 | 0.77 | 0.79 | 103 | empty |
| 2 | 1169 | 0.75 | 0.78 | 102 | empty |
| 3 | 351 | 0.56 | 0.75 | 38 | empty |
| 4 | 299 | 0.54 | 0.75 | 44 | empty |
| 5 | 59 | 0.50 | 0.86 | 18 | empty |
Interfaces
19 interfaces between chains.
- G–H · 1602 Ų buried · 24 hydrogen bonds · protein-protein
- B–F · 1547 Ų buried · 41 hydrogen bonds · protein-protein
- E–F · 1512 Ų buried · 23 hydrogen bonds · protein-protein
- A–G · 1487 Ų buried · 32 hydrogen bonds · protein-protein
- D–H · 1421 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 1GO4 · Crystal structure of Mad1-Mad2 reveals a conserved Mad2 binding motif in Mad1 and Cdc20. · the same entry in another collection · chain H against H, TM-score 1.00
- Q13257 · AlphaFold monomer V2.0 prediction for mitotic spindle assembly checkpoint protein MAD2A… · a predicted model of the same protein · chain B against A, TM-score 0.98
- Q9Y6D9 · AlphaFold monomer V2.0 prediction for mitotic spindle assembly checkpoint protein MAD1… · a predicted model of the same protein · chain H against A, TM-score 0.55
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 Q13257
- Every structure of UniProt Q9Y6D9
- Elsewhere: RCSB PDB 1GO4 · PDBe 1GO4 · UniProt Q13257 · UniProt Q9Y6D9
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