Research workbench
DNA polymerase IV - DNA ternary complex 5
Analyse DNA polymerase IV - DNA ternary complex 5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YUV
- Type
- protein + DNA
- Length
- 753 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase IV; DTN1; DTN2
- EC
- 2.7.7.7
- UniProt
- Q47155
- Ligands
- TTP, MG
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, A | DNA polymerase IV (EC 2.7.7.7) | protein | 342 | 42% helix, 23% strand | Q47155 |
| G, B | DTN1 | dna | 18 | — | — |
| H | DTN2 | dna | 16 | — | — |
| C | DTN1 | dna | 17 | — | — |
Ligands and binding sites
- TTP · Thymidine-5'-triphosphate · ligand · 2 copies · chains F, G, H, A, B, C
- MG · Magnesium ion · metal · 4 copies · chains F, H, A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1033 | 0.81 | 0.83 | 86 | MG, TTP |
| 2 | 1086 | 0.80 | 0.81 | 82 | MG, TTP |
| 3 | 721 | 0.75 | 0.81 | 54 | empty |
| 4 | 652 | 0.75 | 0.82 | 50 | empty |
| 5 | 76 | 0.36 | 0.76 | 15 | empty |
Interfaces
9 interfaces between chains.
- A–B · 1014 Ų buried · 24 hydrogen bonds · protein-nucleic
- F–G · 966 Ų buried · 22 hydrogen bonds · protein-nucleic
- B–C · 651 Ų buried · 63 hydrogen bonds · nucleic-nucleic
- G–H · 644 Ų buried · 62 hydrogen bonds · nucleic-nucleic
- A–C · 575 Ų buried · 20 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 Q47155
- Elsewhere: RCSB PDB 5YUV · PDBe 5YUV · UniProt Q47155
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