Research workbench
Interleukin-8, mutant with glu 38 replaced by cys and cys 50 replaced by ala
Analyse Interleukin-8, mutant with glu 38 replaced by cys and cys 50 replaced by ala in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ICW
- Type
- protein
- Length
- 135 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-8
- UniProt
- P10145
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-8 | protein | 69 | 25% helix, 25% strand | P10145 |
| B | Interleukin-8 | protein | 66 | 27% helix, 29% strand | P10145 |
Interfaces
1 interface between chains.
- A–B · 1082 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1ICW · Interleukin-8, mutant with glu 38 replaced by cys and cys 50 replaced by ala · the same entry in another collection · chain A against A, TM-score 1.00
- P10145 · AlphaFold monomer V2.0 prediction for interleukin-8 (P10145) · a predicted model of the same protein · chain B against A, TM-score 0.92
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 1ICW · PDBe 1ICW · UniProt P10145
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