Research workbench
Crystal structure of recombinant human platelet factor 4
Analyse Crystal structure of recombinant human platelet factor 4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RHP
- Type
- protein
- Length
- 256 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Platelet factor 4
- UniProt
- P02776
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Platelet factor 4 | protein | 64 | 20% helix, 25% strand | P02776 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 444 | 0.81 | 0.89 | 55 | empty |
| 2 | 71 | 0.35 | 0.76 | 11 | empty |
Interfaces
6 interfaces between chains.
- A–C · 971 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 885 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 826 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 613 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 182 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
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 P02776
- Elsewhere: RCSB PDB 1RHP · PDBe 1RHP · UniProt P02776
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