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 1-15 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
- 1PFM
- 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
- 5 · best druggability 0.80
Structure
solution nmr · 1 distinct chain · 16% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | PF4-M2 chimera | protein | 68 | 16% helix, 21% strand | P02776 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 615 | 0.80 | 0.86 | 92 | empty |
| 2 | 57 | 0.67 | 0.94 | 27 | empty |
| 3 | 187 | 0.53 | 0.78 | 39 | empty |
| 4 | 117 | 0.48 | 0.79 | 22 | empty |
| 5 | 69 | 0.37 | 0.78 | 21 | empty |
Interfaces
6 interfaces between chains.
- C–D · 730 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 725 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 578 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 525 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 161 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 1PFM · 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 0.79
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 1PFM · PDBe 1PFM · UniProt P02776
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