Research workbench
NMR structure of the membrane-binding domain of CTP phosphocholine cytidylyltransferase, 10 structures
Analyse NMR structure of the membrane-binding domain of CTP phosphocholine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PEI
- Type
- protein
- Length
- 22 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PEPC22
- EC
- 2.7.7.15
- UniProt
- P19836
- Ligands
- ACE, NH2
Structure
solution nmr · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PEPC22 (EC 2.7.7.15) | protein | 22 | 73% helix, 0% strand | P19836 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1PEI · NMR structure of the membrane-binding domain of CTP phosphocholine cytidylyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
- P19836 · AlphaFold monomer V2.0 prediction for choline-phosphate cytidylyltransferase a (P19836) · a predicted model of the same protein · chain A against A, TM-score 0.40
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 P19836
- Elsewhere: RCSB PDB 1PEI · PDBe 1PEI · UniProt P19836
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