MolNFT v1 · #74897 · protein
Structure of the N-terminal brct domain of human microcephalin (MCPH1)
3PA6: “Structure of the N-terminal brct domain of human microcephalin (MCPH1)”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.25). MolNFT v1 #74897 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3PA6
- Type
- protein
- Length
- 287 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microcephalin
- UniProt
- Q8NEM0
- Ligands
- CL
- Pockets
- 1 · best druggability 0.25
Structure
x-ray diffraction · 3 distinct chains · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Microcephalin | protein | 99 | 33% helix, 19% strand | Q8NEM0 |
| B | Microcephalin | protein | 96 | 34% helix, 20% strand | Q8NEM0 |
| C | Microcephalin | protein | 92 | 36% helix, 21% strand | Q8NEM0 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.25 | 0.73 | 14 | empty |
Interfaces
2 interfaces between chains.
- A–C · 420 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 404 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (engineered).
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 Q8NEM0
- Elsewhere: RCSB PDB 3PA6 · PDBe 3PA6 · UniProt Q8NEM0
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