Research workbench
Oligomeric structure of the chemokine CCL5/RANTES from NMR, ms, and saxs data
Analyse Oligomeric structure of the chemokine CCL5/RANTES from NMR, ms, and saxs data in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L9H
- Type
- protein
- Length
- 264 residues
- Chains
- 4
- Method
- solution nmr; solution scattering
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13501
Structure
solution nmr; solution scattering · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 67 | — | P13501 |
| B, D | — | protein | 65 | — | P13501 |
Compared structures
- 2L9H · Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data · the same entry in another collection · chain D against D, TM-score 1.00
- P13501 · AlphaFold monomer V2.0 prediction for C-C motif chemokine 5 (P13501) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P13501
- Elsewhere: RCSB PDB 2L9H · PDBe 2L9H · UniProt P13501
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