Research workbench
Crystal structure of the complex between SCPA(RESIDUES 1-160)- SCPB(RESIDUES 1-183)
Analyse Crystal structure of the complex between SCPA(RESIDUES 1-160)- SCPB(RESIDUES… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I98
- Type
- protein
- Length
- 480 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Segregation and condensation protein a; Segregation and condensation protein B
- UniProt
- C1CMI6, C1CMI5
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 56% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Segregation and condensation protein a | protein | 147 | 63% helix, 0% strand | C1CMI6 |
| B | Segregation and condensation protein B | protein | 167 | 53% helix, 16% strand | C1CMI5 |
| C | Segregation and condensation protein B | protein | 166 | 54% helix, 13% strand | C1CMI5 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 973 | 0.78 | 0.80 | 80 | empty |
| 2 | 152 | 0.56 | 0.81 | 17 | empty |
| 3 | 85 | 0.53 | 0.84 | 20 | empty |
| 4 | 130 | 0.42 | 0.75 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–C · 2037 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 1652 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 1422 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 4I98 · Crystal structure of the complex between ScpA(residues 1-160)-ScpB(residues 1-183) · the same entry in another collection · chain C against C, TM-score 1.00
- C1CMI6 · AlphaFold monomer V2.0 prediction for segregation and condensation protein a (C1CMI6) · a predicted model of the same protein · chain A against A, TM-score 0.94
- C1CMI5 · AlphaFold monomer V2.0 prediction for segregation and condensation protein B (C1CMI5) · a predicted model of the same protein · chain C against A, TM-score 0.93
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 C1CMI6
- Every structure of UniProt C1CMI5
- Elsewhere: RCSB PDB 4I98 · PDBe 4I98 · UniProt C1CMI6 · UniProt C1CMI5
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