MolNFT v1 · #170678 · protein
Lamin a 17-70 COIL1A dimer stabilized by C-terminal capping
6YF5 · Prelamin-A/C,MICROTUBULE-associated protein RP/EB family…: “Lamin a 17-70 COIL1A dimer stabilized by C-terminal capping”. X-ray diffraction, 2 pockets (best druggability 0.72). MolNFT v1 #170678 on GenesisL1: 3D structure, binding…
- PDB
- 6YF5
- Type
- protein
- Length
- 341 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prelamin-A/C,MICROTUBULE-associated protein RP/EB family member 1
- UniProt
- P02545, Q15691
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 84% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prelamin-A/C,MICROTUBULE-associated protein RP/EB family member 1 | protein | 89 | 81% helix, 3% strand | P02545, Q15691 |
| B | Prelamin-A/C,MICROTUBULE-associated protein RP/EB family member 1 | protein | 83 | 88% helix, 4% strand | P02545, Q15691 |
| C | Prelamin-A/C,MICROTUBULE-associated protein RP/EB family member 1 | protein | 87 | 79% helix, 1% strand | P02545, Q15691 |
| D | Prelamin-A/C,MICROTUBULE-associated protein RP/EB family member 1 | protein | 82 | 89% helix, 1% strand | P02545, Q15691 |
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 | 693 | 0.72 | 0.78 | 64 | empty |
| 2 | 77 | 0.44 | 0.81 | 16 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2486 Ų buried · 32 hydrogen bonds · protein-protein
- A–B · 2462 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 313 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 292 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 219 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 P02545
- Every structure of UniProt Q15691
- Elsewhere: RCSB PDB 6YF5 · PDBe 6YF5 · UniProt P02545 · UniProt Q15691
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