Research workbench
The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-ångströms resolution
Analyse The crystal structure of recombinant human neutrophil-activating peptide-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NAP
- Type
- protein
- Length
- 261 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neutrophil activating peptide-2
- UniProt
- P02775
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Neutrophil activating peptide-2 | protein | 66 | 21% helix, 30% strand | P02775 |
| C | Neutrophil activating peptide-2 | protein | 63 | 21% helix, 32% strand | P02775 |
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 | 522 | 0.82 | 0.89 | 76 | empty |
| 2 | 60 | 0.34 | 0.77 | 13 | empty |
Interfaces
6 interfaces between chains.
- C–D · 793 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 777 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 708 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 697 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 117 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 1NAP · The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at… · the same entry in another collection · chain D against D, TM-score 1.00
- P02775 · AlphaFold monomer V2.0 prediction for platelet basic protein (P02775) · a predicted model of the same protein · chain C against A, TM-score 0.93
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 P02775
- Elsewhere: RCSB PDB 1NAP · PDBe 1NAP · UniProt P02775
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