Research workbench
Identification of small molecule inhibitors selective for APO(A) kringles kiv-7, kiv-10 and kv.
Analyse Identification of small molecule inhibitors selective for APO(A) kringles… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BVD
- Type
- protein
- Length
- 78 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- APOLIPOPROTEIN(A)
- EC
- 3.4.21.-
- UniProt
- P08519
- Ligands
- BU6, CL
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | APOLIPOPROTEIN(A) (EC 3.4.21.-) | protein | 78 | 0% helix, 19% strand | P08519 |
Ligands and binding sites
- BU6 · 5-chloro-2-fluoro-N-[1-(4-piperidyl)pyrazol-4-yl]benzenesulfonamide · ligand · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 4BVD · Identification of small molecule inhibitors selective for apo(a) kringles KIV-7, KIV-10… · 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 P08519
- Elsewhere: RCSB PDB 4BVD · PDBe 4BVD · UniProt P08519
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