Research workbench
Structural basis of receptor sulfotyrosine recognition by a cc chemokine: the N-terminal region of CCR3 bound to CCL11/EOTAXIN-1
Analyse Structural basis of receptor sulfotyrosine recognition by a cc chemokine: the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MPM
- Type
- protein
- Length
- 90 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eotaxin; CCR3
- UniProt
- P51671
Structure
solution nmr · 2 distinct chains · 13% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eotaxin | protein | 74 | 16% helix, 12% strand | P51671 |
| B | CCR3 | protein | 16 | 0% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 614 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 modified (disulfide, sulfation).
Compared structures
- 2MPM · Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: the N-terminal… · the same entry in another collection · chain A against A, TM-score 1.00
- P51671 · AlphaFold monomer V2.0 prediction for eotaxin (P51671) · a predicted model of the same protein · chain A against A, TM-score 0.68
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 P51671
- Elsewhere: RCSB PDB 2MPM · PDBe 2MPM · UniProt P51671
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