Research workbench
Structure of human immunodeficiency virus type 1 VPR(34-51) peptide in aqueous tfe solution
Analyse Structure of human immunodeficiency virus type 1 VPR(34-51) peptide in aqueous… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KZS
- Type
- protein
- Length
- 18 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vpr protein
- UniProt
- P12520
- Ligands
- ACE, NH2
Structure
solution nmr · 1 distinct chain · 89% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vpr protein | protein | 18 | 89% helix, 0% strand | P12520 |
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
- 1KZS · Structure of Human Immunodeficiency Virus Type 1 Vpr(34-51) Peptide in Aqueous TFE… · 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 P12520
- Elsewhere: RCSB PDB 1KZS · PDBe 1KZS · UniProt P12520
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