MolNFT v1 · #125991 · protein
Structure of the zinc finger array of CEP104
5LPI · Centrosomal protein of 104 kda: “Structure of the zinc finger array of CEP104”. X-ray diffraction, 1 ligand (ZN), 10 pockets (best druggability 0.69). MolNFT v1 #125991 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5LPI
- Type
- protein
- Length
- 529 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Centrosomal protein of 104 kda
- UniProt
- O60308
- Ligands
- ZN
- Pockets
- 10 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, B | Centrosomal protein of 104 kda | protein | 133 | 31% helix, 14% strand | O60308 |
| C | Centrosomal protein of 104 kda | protein | 134 | 31% helix, 13% strand | O60308 |
| A | Centrosomal protein of 104 kda | protein | 129 | 30% helix, 14% strand | O60308 |
Ligands and binding sites
- ZN · Zinc ion · metal · 16 copies · chains D, C, A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 558 | 0.69 | 0.78 | 45 | empty |
| 2 | 573 | 0.69 | 0.78 | 56 | empty |
| 3 | 314 | 0.61 | 0.78 | 34 | empty |
| 4 | 291 | 0.56 | 0.76 | 34 | empty |
| 5 | 176 | 0.47 | 0.76 | 31 | empty |
Interfaces
5 interfaces between chains.
- A–B · 537 Ų buried · 8 hydrogen bonds · protein-protein
- D–A · 488 Ų buried · 5 hydrogen bonds · protein-protein
- C–A · 430 Ų buried · 3 hydrogen bonds · protein-protein
- C–B · 129 Ų buried · 1 hydrogen bond · protein-protein
- D–C · 110 Ų buried · 5 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 O60308
- Elsewhere: RCSB PDB 5LPI · PDBe 5LPI · UniProt O60308
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