Research workbench
Homonuclear 1H nuclear magnetic resonance assignment and structural characterization of HIV-1 tat mal protein
Analyse Homonuclear 1H nuclear magnetic resonance assignment and structural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K5K
- Type
- protein
- Length
- 87 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tat protein
- UniProt
- P04613
Structure
solution nmr · 1 distinct chain · 5% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tat protein | protein | 87 | 5% helix, 0% strand | P04613 |
Compared structures
- 1K5K · Homonuclear 1H Nuclear Magnetic Resonance Assignment and Structural Characterization of… · 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 P04613
- Elsewhere: RCSB PDB 1K5K · PDBe 1K5K · UniProt P04613
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