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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 I
Analyse Crystal structures of the ADP and ATP bound forms of the bacillus anti-sigma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TID
- Type
- protein
- Length
- 507 residues
- Chains
- 4
- 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
- 8 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 42% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anti-sigma F factor (EC 2.7.1.37) | protein | 136 | 38% helix, 28% strand | O32727 |
| B | Anti-sigma F factor antagonist | protein | 119 | 45% helix, 29% strand | O32726 |
| C | Anti-sigma F factor (EC 2.7.1.37) | protein | 134 | 41% helix, 28% strand | O32727 |
| D | Anti-sigma F factor antagonist | protein | 118 | 44% helix, 31% strand | O32726 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.73 | 0.90 | 43 | MG, ATP |
| 2 | 200 | 0.71 | 0.88 | 39 | MG, ATP |
| 3 | 69 | 0.47 | 0.83 | 16 | empty |
| 4 | 69 | 0.42 | 0.80 | 21 | empty |
| 5 | 51 | 0.39 | 0.81 | 15 | empty |
Interfaces
3 interfaces between chains.
- C–D · 901 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 897 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 727 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 19 modified (engineered).
Compared structures
- 1TID · Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor… · the same entry in another collection · chain D against D, TM-score 1.00
- O32727 · AlphaFold monomer V2.0 prediction for anti-sigma F factor (O32727) · a predicted model of the same protein · chain C 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 D against A, TM-score 0.96
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 1TID · PDBe 1TID · UniProt O32727 · UniProt O32726
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