MolNFT v1 · #176244 · protein
NSE1-NSE3-NSE4 complex
7DG2 · Non-structural maintenance of chromosomes element 1 homolog: “NSE1-NSE3-NSE4 complex”. X-ray diffraction, 1 ligand (ZN), 4 pockets (best druggability 0.70). MolNFT v1 #176244 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7DG2
- Type
- protein
- Length
- 492 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-structural maintenance of chromosomes element 1 homolog; Mage domain-containing…
- EC
- 2.3.2.27
- UniProt
- Q6PAF4, A0A1L8G3Z0, B1WBD6
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-structural maintenance of chromosomes element 1 homolog (EC 2.3.2.27) | protein | 231 | 45% helix, 16% strand | Q6PAF4 |
| C | Mage domain-containing protein | protein | 207 | 56% helix, 14% strand | A0A1L8G3Z0 |
| D | Non-structural maintenance of chromosomes element 4 | protein | 54 | 41% helix, 2% strand | B1WBD6 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
- ACT · Acetate ion · additive · 2 copies · chains A, C, D
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 374 | 0.70 | 0.83 | 46 | ACT, GOL |
| 2 | 181 | 0.57 | 0.81 | 29 | empty |
| 3 | 59 | 0.35 | 0.79 | 14 | empty |
| 4 | 54 | 0.28 | 0.74 | 13 | empty |
Interfaces
3 interfaces between chains.
- C–D · 2277 Ų buried · 30 hydrogen bonds · protein-protein
- A–C · 1335 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 969 Ų buried · 11 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 Q6PAF4
- Every structure of UniProt A0A1L8G3Z0
- Every structure of UniProt B1WBD6
- Elsewhere: RCSB PDB 7DG2 · PDBe 7DG2 · UniProt Q6PAF4 · UniProt A0A1L8G3Z0 · UniProt B1WBD6
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