Research workbench
Crystal structure and biochemical characterization of recombinant human calcyphosine delineates a novel ef-hand-containing protein family
Analyse Crystal structure and biochemical characterization of recombinant human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E3R
- Type
- protein
- Length
- 358 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q13938
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 183 | — | Q13938 |
| B | — | protein | 175 | — | Q13938 |
Compared structures
- 3E3R · Crystal structure and biochemical characterization of recombinant human calcyphosine… · the same entry in another collection · chain A against A, TM-score 1.00
- Q13938 · AlphaFold monomer V2.0 prediction for calcyphosin (Q13938) · a predicted model of the same protein · chain B against A, TM-score 0.89
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 Q13938
- Elsewhere: RCSB PDB 3E3R · PDBe 3E3R · UniProt Q13938
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.