Research workbench
The apo structure of nrs-1 C terminal region (305-718)
Analyse The apo structure of nrs-1 C terminal region (305-718) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6K9C
- Type
- protein
- Length
- 830 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Primase
- UniProt
- M5AAG8
- Ligands
- HG, SO4
- Pockets
- 9 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Primase | protein | 416 | 41% helix, 20% strand | M5AAG8 |
| B | Primase | protein | 414 | 41% helix, 20% strand | M5AAG8 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1133 | 0.82 | 0.83 | 90 | SO4 |
| 2 | 935 | 0.78 | 0.81 | 84 | SO4 |
| 3 | 204 | 0.49 | 0.76 | 31 | empty |
| 4 | 157 | 0.46 | 0.76 | 25 | empty |
| 5 | 120 | 0.45 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2270 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 6K9C · The apo structure of NrS-1 C terminal region (305-718) · the same entry in another collection · chain A against A, TM-score 1.00
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 M5AAG8
- Elsewhere: RCSB PDB 6K9C · PDBe 6K9C · UniProt M5AAG8
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