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Structure of the N-terminal domain of fop (FGFR1OP) protein
Analyse Structure of the N-terminal domain of fop (FGFR1OP) protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2D68
- Type
- protein
- Length
- 152 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fop
- UniProt
- O95684
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fop | protein | 75 | 65% helix, 0% strand | O95684 |
| B | Fop | protein | 77 | 69% helix, 0% strand | O95684 |
Interfaces
1 interface between chains.
- A–B · 1515 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
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 O95684
- Elsewhere: RCSB PDB 2D68 · PDBe 2D68 · UniProt O95684
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