Research workbench
NMR structure of the transmembrane and cytoplasmic domains of human CD4
Analyse NMR structure of the transmembrane and cytoplasmic domains of human CD4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KLU
- Type
- protein
- Length
- 70 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-cell surface glycoprotein CD4
- UniProt
- P01730
Structure
solution nmr · 1 distinct chain · 44% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-cell surface glycoprotein CD4 | protein | 70 | 44% helix, 0% strand | P01730 |
Compared structures
- 2KLU · NMR structure of the transmembrane and cytoplasmic domains of human CD4 · the same entry in another collection · chain A against A, TM-score 1.00
- P01730 · AlphaFold monomer V2.0 prediction for T-cell surface glycoprotein CD4 (P01730) · a predicted model of the same protein · chain A against A, TM-score 0.35
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 P01730
- Elsewhere: RCSB PDB 2KLU · PDBe 2KLU · UniProt P01730
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