MolNFT v1 · #22860 · protein
Crystal structures of the ADP and ATP bound forms of the bacillus anti-sigma factor spoiiab in complex with the anti-anti-sigma SPOIIAA:POISED for phosphorylation complex with ATP, crystal form II
1TIL · Anti-sigma F factor: “Crystal structures of the ADP and ATP bound forms of the bacillus anti-sigma factor spoiiab in complex with…”. X-ray diffraction, 2 ligands (ATP, MG), 7 pockets (best druggability 0.73). MolNFT v1 #22860 on…
- PDB
- 1TIL
- Type
- protein
- Length
- 774 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-sigma F factor; Anti-sigma F factor antagonist
- EC
- 2.7.1.37
- UniProt
- O32727, O32726
- Ligands
- ATP, MG
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 40% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Anti-sigma F factor (EC 2.7.1.37) | protein | 141 | 37% helix, 30% strand | O32727 |
| B, F | Anti-sigma F factor antagonist | protein | 117 | 43% helix, 32% strand | O32726 |
| D | Anti-sigma F factor antagonist | protein | 118 | 44% helix, 32% strand | O32726 |
| E | Anti-sigma F factor (EC 2.7.1.37) | protein | 140 | 36% helix, 29% strand | O32727 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 3 copies · chains A, B, C, D, E, F
- MG · Magnesium ion · metal · 3 copies · chains A, C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.73 | 0.89 | 35 | MG, ATP |
| 2 | 181 | 0.72 | 0.90 | 32 | MG, ATP |
| 3 | 192 | 0.70 | 0.88 | 34 | MG, ATP |
| 4 | 233 | 0.54 | 0.77 | 34 | empty |
| 5 | 193 | 0.45 | 0.74 | 27 | empty |
Interfaces
7 interfaces between chains.
- C–D · 994 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 968 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 936 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 784 Ų buried · 20 hydrogen bonds · protein-protein
- A–F · 389 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1TIL · Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor… · the same entry in another collection · chain F against F, TM-score 1.00
- O32727 · AlphaFold monomer V2.0 prediction for anti-sigma F factor (O32727) · a predicted model of the same protein · chain E against A, TM-score 0.99
- O32726 · AlphaFold monomer V2.0 prediction for anti-sigma F factor antagonist (O32726) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 O32727
- Every structure of UniProt O32726
- Elsewhere: RCSB PDB 1TIL · PDBe 1TIL · UniProt O32727 · UniProt O32726
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