MolNFT v1 · #97211 · protein
The umuc subunit of the E. COLI DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.
4K74 · DNA polymerase III subunit beta: “The umuc subunit of the E. COLI DNA polymerase V shows a unique interaction with the beta-clamp processivity…”. X-ray diffraction, 7 pockets (best druggability 0.48). MolNFT v1 #97211 on GenesisL1…
- PDB
- 4K74
- Type
- protein
- Length
- 731 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase III subunit beta; Umuc peptide
- EC
- 2.7.7.7
- UniProt
- Q1R4N6, Q8FI25
- Pockets
- 7 · best druggability 0.48
Structure
x-ray diffraction · 4 distinct chains · 21% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA polymerase III subunit beta (EC 2.7.7.7) | protein | 357 | 22% helix, 47% strand | Q1R4N6 |
| B | DNA polymerase III subunit beta (EC 2.7.7.7) | protein | 363 | 21% helix, 46% strand | Q1R4N6 |
| C | Umuc peptide | protein | 5 | 0% helix, 0% strand | Q8FI25 |
| D | Umuc peptide | protein | 6 | 0% helix, 0% strand | Q8FI25 |
Pockets
7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.48 | 0.74 | 35 | empty |
| 2 | 84 | 0.32 | 0.74 | 17 | empty |
| 3 | 55 | 0.31 | 0.76 | 16 | empty |
| 4 | 62 | 0.31 | 0.75 | 13 | empty |
| 5 | 71 | 0.30 | 0.73 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1328 Ų buried · 28 hydrogen bonds · protein-protein
- B–D · 498 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 479 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4K74 · The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the… · 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 Q1R4N6
- Every structure of UniProt Q8FI25
- Elsewhere: RCSB PDB 4K74 · PDBe 4K74 · UniProt Q1R4N6 · UniProt Q8FI25
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