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The first EGF-like domain from human blood coagulation fvii (fucosylated at ser-60), NMR, 20 structures
Analyse The first EGF-like domain from human blood coagulation fvii (fucosylated at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FF7
- Type
- protein
- Length
- 46 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (blood coagulation factor VII)
- UniProt
- P08709
- Ligands
- FUC
Structure
solution nmr · 1 distinct chain · 0% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (blood coagulation factor VII) | protein | 46 | 0% helix, 26% strand | P08709 |
Ligands and binding sites
- FUC · alpha-L-fucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 1 glycan (disulfide, O-glycosylation).
Compared structures
- 1FF7 · The first EGF-like domain from human blood coagulation fvii (fucosylated at ser-60), NMR… · the same entry in another collection · chain A against A, TM-score 1.00
- P08709 · AlphaFold monomer V2.0 prediction for coagulation factor VII (P08709) · a predicted model of the same protein · chain A against A, TM-score 0.65
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 P08709
- Elsewhere: RCSB PDB 1FF7 · PDBe 1FF7 · UniProt P08709
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