Research workbench
PF4-M2 chimeric mutant with the first 10 N-terminal residues of R-PF4 replaced by the N-terminal residues of the IL8 sequence. models 16-27 of a 27-model set.
Analyse PF4-M2 chimeric mutant with the first 10 N-terminal residues of R-PF4 replaced… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PFN
- Type
- protein
- Length
- 272 residues
- Chains
- 4
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PF4-M2 chimera
- UniProt
- P02776
- Pockets
- 4 · best druggability 0.83
Structure
solution nmr · 1 distinct chain · 16% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | PF4-M2 chimera | protein | 68 | 16% helix, 25% strand | P02776 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 827 | 0.83 | 0.86 | 109 | empty |
| 2 | 89 | 0.39 | 0.77 | 18 | empty |
| 3 | 50 | 0.35 | 0.79 | 17 | empty |
| 4 | 53 | 0.31 | 0.75 | 10 | empty |
Interfaces
6 interfaces between chains.
- C–D · 750 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 732 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 413 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 385 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 168 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 1PFN · PF4-M2 chimeric mutant with the first 10 N-terminal residues of R-PF4 replaced by the… · the same entry in another collection · chain A against A, TM-score 1.00
- P02776 · AlphaFold monomer V2.0 prediction for platelet factor 4 (P02776) · a predicted model of the same protein · chain A against A, TM-score 0.77
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 1PFN · PDBe 1PFN · UniProt P02776
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