MolNFT v1 · #187556 · protein
Cryo-EM structure of ACKR3 in complex with CXCL12, an intracellular Fab, and an extracellular Fab
7SK3 · Atypical chemokine receptor 3: “Cryo-EM structure of ACKR3 in complex with CXCL12, an intracellular Fab, and an extracellular Fab”. Electron microscopy, 1 ligand (CLR), 12 pockets (best druggability 0.80). MolNFT v1 #187556 on…
- PDB
- 7SK3
- Type
- protein
- Length
- 831 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Atypical chemokine receptor 3; Stromal cell-derived factor 1; CID25 Fab light chain…
- UniProt
- P25106, P48061
- Ligands
- CLR
- Pockets
- 12 · best druggability 0.80
Structure
electron microscopy · 6 distinct chains · 31% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Atypical chemokine receptor 3 | protein | 304 | 77% helix, 5% strand | P25106 |
| B | Stromal cell-derived factor 1 | protein | 68 | 26% helix, 19% strand | P48061 |
| C | CID25 Fab light chain | protein | 105 | 0% helix, 47% strand | — |
| D | CID25 Fab heavy chain | protein | 123 | 2% helix, 48% strand | — |
| E | CID24 Fab light chain | protein | 106 | 0% helix, 42% strand | — |
| F | CID24 Fab heavy chain | protein | 125 | 5% helix, 50% strand | — |
Ligands and binding sites
- CLR · Cholesterol · ligand · 8 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.80 | 0.96 | 32 | empty |
| 2 | 75 | 0.72 | 0.96 | 20 | empty |
| 3 | 131 | 0.69 | 0.90 | 34 | empty |
| 4 | 133 | 0.60 | 0.85 | 22 | empty |
| 5 | 67 | 0.50 | 0.85 | 18 | empty |
Interfaces
9 interfaces between chains.
- A–B · 1904 Ų buried · 12 hydrogen bonds · protein-protein
- A–F · 1608 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 944 Ų buried · 2 hydrogen bonds · protein-protein
- E–F · 936 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 927 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 7SK3 · Cryo-EM structure of ACKR3 in complex with CXCL12, an intracellular Fab, and an… · the same entry in another collection · chain F against F, TM-score 1.00
- P25106 · AlphaFold monomer V2.0 prediction for atypical chemokine receptor 3 (P25106) · a predicted model of the same protein · chain A against A, TM-score 0.93
- P48061 · AlphaFold monomer V2.0 prediction for stromal cell-derived factor 1 (P48061) · a predicted model of the same protein · chain B against A, TM-score 0.79
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 P25106
- Every structure of UniProt P48061
- Elsewhere: RCSB PDB 7SK3 · PDBe 7SK3 · UniProt P25106 · UniProt P48061
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