Research workbench
Mechanistic implications for the bacterial primosome assembly of the structure of a helicase-helicase loader complex
Analyse Mechanistic implications for the bacterial primosome assembly of the structure… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M4W
- Type
- protein
- Length
- 4,043 residues
- Chains
- 15
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Replicative helicase; DNA primase; Primosomal protein dnai
- UniProt
- Q9X4C9, Q9X4D0, P06567
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 8 distinct chains · 19% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Replicative helicase | protein | 358 | 24% helix, 9% strand | Q9X4C9 |
| G, H, I | DNA primase | protein | 138 | 33% helix, 0% strand | Q9X4D0 |
| J | Primosomal protein dnai | protein | 245 | 13% helix, 14% strand | P06567 |
| K | Primosomal protein dnai | protein | 248 | 17% helix, 10% strand | P06567 |
| L | Primosomal protein dnai | protein | 247 | 18% helix, 12% strand | P06567 |
| M | Primosomal protein dnai | protein | 247 | 17% helix, 10% strand | P06567 |
| N | Primosomal protein dnai | protein | 244 | 14% helix, 10% strand | P06567 |
| O | Primosomal protein dnai | protein | 250 | 19% helix, 16% strand | P06567 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 922 | 0.83 | 0.85 | 116 | empty |
| 2 | 1136 | 0.81 | 0.82 | 108 | empty |
| 3 | 129 | 0.79 | 0.96 | 31 | empty |
| 4 | 1199 | 0.79 | 0.80 | 127 | empty |
| 5 | 137 | 0.78 | 0.95 | 24 | empty |
Interfaces
33 interfaces between chains.
- E–F · 1385 Ų buried · 23 hydrogen bonds · protein-protein
- A–D · 1319 Ų buried · 4 hydrogen bonds · protein-protein
- B–E · 1246 Ų buried · 14 hydrogen bonds · protein-protein
- M–N · 1061 Ų buried · 17 hydrogen bonds · protein-protein
- L–M · 989 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 4M4W · Mechanistic implications for the bacterial primosome assembly of the structure of a… · the same entry in another collection · chain O against O, 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 Q9X4C9
- Every structure of UniProt Q9X4D0
- Every structure of UniProt P06567
- Elsewhere: RCSB PDB 4M4W · PDBe 4M4W · UniProt Q9X4C9 · UniProt Q9X4D0 · UniProt P06567
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