MolNFT v1 · #33239 · protein
Phosphorylation of the cytoplasmic tail of tissue factor and its role in modulating structure and binding affinity
2CEH: “Phosphorylation of the cytoplasmic tail of tissue factor and its role in modulating structure and binding…”. Solution nmr. MolNFT v1 #33239 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
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