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Crystal structure of human chymase in complex with fragment inhibitor 6-chloro-1,3-dihydro-2H-indol-2-one
Analyse Crystal structure of human chymase in complex with fragment inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K2Y
- Type
- protein
- Length
- 217 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
- ES2, NAG, ZN
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chymase (EC 3.4.21.39) | protein | 217 | 9% helix, 38% strand | P23946 |
Ligands and binding sites
- ES2 · 6-chloro-1,3-dihydro-2H-indol-2-one · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- ZN · Zinc ion · metal · 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 | 191 | 0.50 | 0.77 | 40 | ES2 |
| 2 | 57 | 0.34 | 0.77 | 13 | empty |
Modifications
Observed in the structure: 3 disulfide, 1 glycan (disulfide, N-glycosylation).
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 4K2Y · PDBe 4K2Y · UniProt P23946
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