MolNFT v1 · #14961 · protein
Structure of BHPBR3, the baff-binding loop of BR3 embedded in a beta- hairpin peptide
1MPV · Blys receptor 3: “Structure of BHPBR3, the baff-binding loop of BR3 embedded in a beta- hairpin peptide”. Solution nmr, 2 ligands (ACE, NH2). MolNFT v1 #14961 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MPV
- Type
- protein
- Length
- 12 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Blys receptor 3
- UniProt
- Q96RJ3
- Ligands
- ACE, NH2
Structure
solution nmr · 1 distinct chain · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Blys receptor 3 | protein | 12 | 0% helix, 50% strand | Q96RJ3 |
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, 1 disulfide (covalent ligand, disulfide).
Compared structures
- 1MPV · Structure of bhpBR3, the BAFF-binding loop of BR3 embedded in a beta-hairpin peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q96RJ3 · AlphaFold monomer V2.0 prediction for tumor necrosis factor receptor superfamily member… · a predicted model of the same protein · chain A against A, TM-score 0.67
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 Q96RJ3
- Elsewhere: RCSB PDB 1MPV · PDBe 1MPV · UniProt Q96RJ3
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