Research workbench
Bifunctional dctp DEAMINASE:DUTPASE from mycobacterium tuberculosis, apo form
Analyse Bifunctional dctp DEAMINASE:DUTPASE from mycobacterium tuberculosis, apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QLP
- Type
- protein
- Length
- 956 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deoxycytidine triphosphate deaminase
- EC
- 3.5.4.13
- UniProt
- O07247
- Pockets
- 16 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 11% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deoxycytidine triphosphate deaminase (EC 3.5.4.13) | protein | 161 | 12% helix, 40% strand | O07247 |
| B, C, E | Deoxycytidine triphosphate deaminase (EC 3.5.4.13) | protein | 159 | 9% helix, 43% strand | O07247 |
| D | Deoxycytidine triphosphate deaminase (EC 3.5.4.13) | protein | 160 | 12% helix, 41% strand | O07247 |
| F | Deoxycytidine triphosphate deaminase (EC 3.5.4.13) | protein | 158 | 10% helix, 41% strand | O07247 |
Ligands and binding sites
- 1PE · Pentaethylene glycol · additive · 7 copies · chains A, C, B, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1042 | 0.87 | 0.89 | 137 | empty |
| 2 | 81 | 0.77 | 0.99 | 22 | empty |
| 3 | 265 | 0.64 | 0.81 | 33 | empty |
| 4 | 276 | 0.63 | 0.81 | 45 | empty |
| 5 | 107 | 0.61 | 0.87 | 23 | empty |
Interfaces
15 interfaces between chains.
- A–B · 1554 Ų buried · 26 hydrogen bonds · protein-protein
- D–E · 1552 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1538 Ų buried · 19 hydrogen bonds · protein-protein
- E–F · 1533 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 1484 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 2QLP · Bifunctional dCTP deaminase:dUTPase from Mycobacterium tuberculosis, apo form · 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 O07247
- Elsewhere: RCSB PDB 2QLP · PDBe 2QLP · UniProt O07247
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