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The 1.5 a crystal structure of CA2+-bound S100A4
Analyse The 1.5 a crystal structure of CA2+-bound S100A4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C1V
- Type
- protein
- Length
- 380 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein S100-A4
- UniProt
- P26447
- Ligands
- CA
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Protein S100-A4 | protein | 93 | 65% helix, 4% strand | P26447 |
| B, D | Protein S100-A4 | protein | 97 | 62% helix, 4% strand | P26447 |
Ligands and binding sites
- CA · Calcium ion · metal · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 278 | 0.53 | 0.75 | 38 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1517 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1508 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 899 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 P26447
- Elsewhere: RCSB PDB 3C1V · PDBe 3C1V · UniProt P26447
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