Research workbench
Phosphorylation of the cytoplasmic tail of tissue factor and its role in modulating structure and binding affinity
Analyse Phosphorylation of the cytoplasmic tail of tissue factor and its role in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CEH
- Type
- protein
- Length
- 19 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13726
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 19 | — | P13726 |
Compared structures
- 2CEH · Phosphorylation of the Cytoplasmic Tail of Tissue Factor and its Role in Modulating… · the same entry in another collection · chain A against A, TM-score 1.00
- P13726 · AlphaFold monomer V2.0 prediction for tissue factor (P13726) · a predicted model of the same protein · chain A against A, TM-score 0.17
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 P13726
- Elsewhere: RCSB PDB 2CEH · PDBe 2CEH · UniProt P13726
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.