Research workbench
Structural changes induced in apo-S100A1 protein by the disulphide formation between its CYS85 residue and B-mercaptoethanol
Analyse Structural changes induced in apo-S100A1 protein by the disulphide formation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JPT
- Type
- protein
- Length
- 186 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein S100-A1
- UniProt
- P02639
- Pockets
- 4 · best druggability 0.56
Structure
solution nmr · 1 distinct chain · 62% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein S100-A1 | protein | 93 | 62% helix, 4% strand | P02639 |
Ligands and binding sites
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.56 | 0.87 | 17 | empty |
| 2 | 68 | 0.52 | 0.85 | 16 | empty |
| 3 | 115 | 0.43 | 0.77 | 22 | empty |
| 4 | 94 | 0.39 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1472 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 2JPT · Structural changes induced in apo-s100a1 protein by the disulphide formation between its… · the same entry in another collection · chain A against A, TM-score 1.00
- P02639 · AlphaFold monomer V2.0 prediction for protein S100-A1 (P02639) · a predicted model of the same protein · chain A against A, TM-score 0.56
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 P02639
- Elsewhere: RCSB PDB 2JPT · PDBe 2JPT · UniProt P02639
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