MolNFT v1 · #28721 · protein
Signal transduction protein chey mutant with phe 14 replaced by gly, ser 15 replaced by gly, and met 17 replaced by gly
1YMV: “Signal transduction protein chey mutant with phe 14 replaced by gly, ser 15 replaced by gly, and met 17…”. X-ray diffraction, 1 ligand (MG). MolNFT v1 #28721 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1YMV
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chey
- UniProt
- P06143
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chey | protein | 124 | 46% helix, 19% strand | P06143 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1YMV · Signal transduction protein chey mutant with phe 14 replaced by gly, ser 15 replaced by… · the same entry in another collection · chain A against A, TM-score 1.00
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 P06143
- Elsewhere: RCSB PDB 1YMV · PDBe 1YMV · UniProt P06143
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