Research workbench
Solution structure of the human cc chemokine, I-309
Analyse Solution structure of the human cc chemokine, I-309 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EL0
- Type
- protein
- Length
- 74 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- I-309
- UniProt
- P22362
Structure
solution nmr · 1 distinct chain · 15% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | I-309 | protein | 74 | 15% helix, 22% strand | P22362 |
Modifications
Observed in the structure: 3 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 P22362
- Elsewhere: RCSB PDB 1EL0 · PDBe 1EL0 · UniProt P22362
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