UniProt E2RHY7
Collagen-binding protein (E2RHY7)
Collagen-binding protein (UniProt E2RHY7): 8 experimental structures on GenesisL1, 1 ligand bound, 43 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- E2RHY7
- Protein
- Collagen-binding protein
- Experimental structures
- 8
- Predicted models
- 0
- Ligands
- 1
- Pockets
- 43 · 3 records with a druggable one
Structures
8 records of E2RHY7 in the MolNFT archive: 8 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 4AU3 | Crystal Structure of a Hsp47-collagen complex | x-ray diffraction | A, B, C, D | — | — |
| 4AU3 | Crystal structure of a HSP47-collagen complex | x-ray diffraction | A, B, C, D | — | — |
| 7BDU | Crystal structure of a Hsp47-collagen peptide complex | x-ray diffraction | A, B | — | 13 (best 0.81) |
| 7BDU | Crystal structure of a HSP47-collagen peptide complex | x-ray diffraction | A, B | ACE | — |
| 7BEE | Crystal structure of a Hsp47-collagen peptide complex | x-ray diffraction | A, B | — | 10 (best 0.84) |
| 7BEE | Crystal structure of a HSP47-collagen peptide complex | x-ray diffraction | A, B | ACE | — |
| 7BFI | A double-histidine mutant of HSP47 slows down client release at low pH | x-ray diffraction | A, C, D, B | — | 20 (best 0.76) |
| 7BFI | A double-histidine mutant of HSP47 slows down client release at low pH | x-ray diffraction | A, C, D, B | — | — |
Ligands
- ACE · Acetyl group · in 2 records
Elsewhere
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