Research workbench
Crystal structure of human KLK4 and SPINK2 derived KLK4 inhibitor complex
Analyse Crystal structure of human KLK4 and SPINK2 derived KLK4 inhibitor complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KBR
- Type
- protein
- Length
- 278 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kallikrein-4; K41043
- EC
- 3.4.21.-
- UniProt
- Q9Y5K2
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kallikrein-4 (EC 3.4.21.-) | protein | 223 | 10% helix, 37% strand | Q9Y5K2 |
| C | K41043 | protein | 55 | 25% helix, 20% strand | — |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 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 | 0.41 | 0.75 | 20 | empty |
| 2 | 122 | 0.41 | 0.76 | 21 | empty |
Interfaces
1 interface between chains.
- A–C · 885 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
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 Q9Y5K2
- Elsewhere: RCSB PDB 6KBR · PDBe 6KBR · UniProt Q9Y5K2
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