Research workbench
Solution structure and dynamics of human S100A1 protein modified at cysteine 85 with homocysteine disulfide bond formation in calcium saturated form
Analyse Solution structure and dynamics of human S100A1 protein modified at cysteine 85… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LP2
- Type
- protein
- Length
- 186 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein S100-A1
- UniProt
- P23297
- Ligands
- HCS, CA
- Pockets
- 1 · best druggability 0.45
Structure
solution nmr · 1 distinct chain · 70% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein S100-A1 | protein | 93 | 70% helix, 4% strand | P23297 |
Ligands and binding sites
- HCS · 2-amino-4-mercapto-butyric acid · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.45 | 0.82 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1504 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 2LP2 · Solution structure and dynamics of human S100A1 protein modified at cysteine 85 with… · the same entry in another collection · chain A against A, TM-score 1.00
- P23297 · AlphaFold monomer V2.0 prediction for protein S100-A1 (P23297) · a predicted model of the same protein · chain B against A, TM-score 0.88
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 P23297
- Elsewhere: RCSB PDB 2LP2 · PDBe 2LP2 · UniProt P23297
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.