Research workbench
Crystal structure of the MOT1 N-terminal domain in complex with tbp
Analyse Crystal structure of the MOT1 N-terminal domain in complex with tbp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OC3
- Type
- protein
- Length
- 1,857 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Helicase MOT1; Transcription initiation factor tfiid (tfiid-1)
- UniProt
- Q8SVZ5, Q8ST28
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 56% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Helicase MOT1 | protein | 752 | 60% helix, 1% strand | Q8SVZ5 |
| B | Helicase MOT1 | protein | 749 | 60% helix, 1% strand | Q8SVZ5 |
| C, D | Transcription initiation factor tfiid (tfiid-1) | protein | 178 | 25% helix, 35% strand | Q8ST28 |
Ligands and binding sites
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 961 | 0.85 | 0.87 | 73 | empty |
| 2 | 1009 | 0.78 | 0.80 | 76 | empty |
| 3 | 474 | 0.74 | 0.82 | 48 | empty |
| 4 | 722 | 0.73 | 0.79 | 59 | empty |
| 5 | 489 | 0.72 | 0.81 | 58 | empty |
Interfaces
4 interfaces between chains.
- B–D · 2033 Ų buried · 29 hydrogen bonds · protein-protein
- A–C · 2018 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 1152 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 548 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3OC3 · Crystal structure of the Mot1 N-terminal domain in complex with TBP · 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 Q8SVZ5
- Every structure of UniProt Q8ST28
- Elsewhere: RCSB PDB 3OC3 · PDBe 3OC3 · UniProt Q8SVZ5 · UniProt Q8ST28
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