Research workbench
Crystal structure of human prostasin complexed to 4-guanidinobenzoic acid
Analyse Crystal structure of human prostasin complexed to 4-guanidinobenzoic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DFL
- Type
- protein
- Length
- 245 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prostasin
- EC
- 3.4.21.-
- UniProt
- Q16651
- Ligands
- GBS
- Pockets
- 3 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prostasin (EC 3.4.21.-) | protein | 245 | 11% helix, 36% strand | Q16651 |
Ligands and binding sites
- GBS · 4-guanidinobenzoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.48 | 0.79 | 30 | GBS |
| 2 | 60 | 0.31 | 0.75 | 15 | empty |
| 3 | 62 | 0.28 | 0.73 | 20 | empty |
Modifications
Observed in the structure: 4 disulfide, 1 covalent (disulfide, covalent ligand).
Compared structures
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 Q16651
- Elsewhere: RCSB PDB 3DFL · PDBe 3DFL · UniProt Q16651
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