Research workbench
Structure of the human csf-1:CSF-1R complex
Analyse Structure of the human csf-1:CSF-1R complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WRM
- Type
- protein
- Length
- 586 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Macrophage colony-stimulating factor 1 receptor; Macrophage colony-stimulating factor 1
- EC
- 2.7.10.1
- UniProt
- P07333, P09603
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Macrophage colony-stimulating factor 1 receptor (EC 2.7.10.1) | protein | 445 | 4% helix, 54% strand | P07333 |
| B | Macrophage colony-stimulating factor 1 | protein | 141 | 52% helix, 9% strand | P09603 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 808 | 0.73 | 0.78 | 64 | empty |
| 2 | 274 | 0.58 | 0.78 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 1066 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 4WRM · Structure of the human CSF-1:CSF-1R complex · the same entry in another collection · chain A against A, TM-score 1.00
- P09603 · AlphaFold monomer V2.0 prediction for macrophage colony-stimulating factor 1 (P09603) · a predicted model of the same protein · chain B against A, TM-score 0.97
- P07333 · AlphaFold monomer V2.0 prediction for macrophage colony-stimulating factor 1 receptor… · a predicted model of the same protein · chain A against A, TM-score 0.54
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 P07333
- Every structure of UniProt P09603
- Elsewhere: RCSB PDB 4WRM · PDBe 4WRM · UniProt P07333 · UniProt P09603
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