Research workbench
Structure of E. COLI dgtpase bound to T7 bacteriophage protein GP1.2
Analyse Structure of E. COLI dgtpase bound to T7 bacteriophage protein GP1.2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7U65
- Type
- protein
- Length
- 3,384 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deoxyguanosinetriphosphate triphosphohydrolase; Inhibitor of dgtpase
- EC
- 3.1.5.1
- UniProt
- P15723, P03780
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 2 distinct chains · 59% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Deoxyguanosinetriphosphate triphosphohydrolase (EC 3.1.5.1) | protein | 481 | 61% helix, 1% strand | P15723 |
| G, H, I, J, K, L | Inhibitor of dgtpase | protein | 83 | 42% helix, 29% strand | P03780 |
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 | 1050 | 0.82 | 0.83 | 80 | empty |
| 2 | 1018 | 0.82 | 0.83 | 75 | empty |
| 3 | 1070 | 0.81 | 0.83 | 79 | empty |
| 4 | 1033 | 0.81 | 0.83 | 74 | empty |
| 5 | 1029 | 0.81 | 0.82 | 78 | empty |
Interfaces
21 interfaces between chains.
- C–D · 1797 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1795 Ų buried · 21 hydrogen bonds · protein-protein
- E–F · 1789 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 654 Ų buried · 7 hydrogen bonds · protein-protein
- D–F · 654 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7U65 · Structure of E. coli dGTPase bound to T7 bacteriophage protein Gp1.2 · the same entry in another collection · chain L against L, 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 P15723
- Every structure of UniProt P03780
- Elsewhere: RCSB PDB 7U65 · PDBe 7U65 · UniProt P15723 · UniProt P03780
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