MolNFT v1 · #109338 · protein + DNA
Crystal structure of the MOT1 N-terminal domain in complex with tbp and NC2 bound to a promoter DNA fragment
4WZS · ECU11_1470 protein: “Crystal structure of the MOT1 N-terminal domain in complex with tbp and NC2 bound to a promoter DNA fragment”. X-ray diffraction, 14 pockets (best druggability 0.74). MolNFT v1 #109338 on GenesisL1: 3D…
- PDB
- 4WZS
- Type
- protein + DNA
- Length
- 1,118 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ECU11_1470 protein; Tata-binding protein-associated phosphoprotein; Similarity to…
- UniProt
- Q8SQT6, M1K2J7, Q8SVZ5, Q8ST28
- Pockets
- 14 · best druggability 0.74
Structure
x-ray diffraction · 6 distinct chains · 56% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ECU11_1470 protein | protein | 66 | 71% helix, 3% strand | Q8SQT6 |
| B | Tata-binding protein-associated phosphoprotein | protein | 113 | 79% helix, 2% strand | M1K2J7 |
| C | Similarity to helicase MOT1 | protein | 722 | 59% helix, 1% strand | Q8SVZ5 |
| D | ECU04_1440 protein | protein | 178 | 26% helix, 33% strand | Q8ST28 |
| E | DNA (5'- D(P*CP*CP*AP*CP*CP*CP*CP*CP*TP*TP*TP*TP*AP*TP*AP*GP*CP*CP*CP*T)-3') | dna | 20 | — | — |
| F | DNA (5'- D(P*GP*GP*GP*CP*TP*AP*TP*AP*AP*AP*AP*GP*GP*GP*GP*GP*TP*GP*G)-3') | dna | 19 | — | — |
Pockets
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 781 | 0.74 | 0.79 | 89 | empty |
| 2 | 815 | 0.73 | 0.78 | 73 | empty |
| 3 | 449 | 0.61 | 0.75 | 44 | empty |
| 4 | 271 | 0.58 | 0.78 | 30 | empty |
| 5 | 52 | 0.52 | 0.88 | 15 | empty |
Interfaces
13 interfaces between chains.
- C–D · 1545 Ų buried · 18 hydrogen bonds · protein-protein
- E–F · 862 Ų buried · 77 hydrogen bonds · nucleic-nucleic
- D–F · 835 Ų buried · 5 hydrogen bonds · protein-nucleic
- D–E · 788 Ų buried · 5 hydrogen bonds · protein-nucleic
- B–D · 711 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 25 modified (engineered).
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 Q8SQT6
- Every structure of UniProt M1K2J7
- Every structure of UniProt Q8SVZ5
- Every structure of UniProt Q8ST28
- Elsewhere: RCSB PDB 4WZS · PDBe 4WZS · UniProt Q8SQT6 · UniProt M1K2J7 · UniProt Q8SVZ5 · UniProt Q8ST28
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