Research workbench
Interleukin-8 with an added disulfide between residues 5 and 33 (L5C/H33C)
Analyse Interleukin-8 with an added disulfide between residues 5 and 33 (L5C/H33C) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QE6
- Type
- protein
- Length
- 278 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-8 variant
- UniProt
- P10145
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 4 distinct chains · 24% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-8 variant | protein | 68 | 25% helix, 25% strand | P10145 |
| B | Interleukin-8 variant | protein | 71 | 24% helix, 27% strand | P10145 |
| C | Interleukin-8 variant | protein | 67 | 25% helix, 25% strand | P10145 |
| D | Interleukin-8 variant | protein | 72 | 24% helix, 26% strand | P10145 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 445 | 0.59 | 0.75 | 51 | empty |
| 2 | 109 | 0.44 | 0.78 | 18 | empty |
| 3 | 66 | 0.31 | 0.75 | 17 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1088 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1079 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 154 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 53 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 35 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 11 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 P10145
- Elsewhere: RCSB PDB 1QE6 · PDBe 1QE6 · UniProt P10145
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