Research workbench
Crystal structure of the human chymase with TJK002
Analyse Crystal structure of the human chymase with TJK002 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KP0
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chymase
- EC
- 3.4.21.39
- UniProt
- P23946
- Ligands
- KPK
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chymase (EC 3.4.21.39) | protein | 220 | 6% helix, 38% strand | P23946 |
Ligands and binding sites
- KPK · 4-({1-[(4-methyl-1-benzothiophen-3-yl)methyl]-1H-benzimidazol-2-yl}sulfanyl)butanoic acid · ligand · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.57 | 0.90 | 16 | empty |
| 2 | 67 | 0.47 | 0.83 | 21 | KPK |
Modifications
Observed in the structure: 3 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 P23946
- Elsewhere: RCSB PDB 4KP0 · PDBe 4KP0 · UniProt P23946
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