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Catalytic domain of stromelysin-1 in complex with N-hydroxy-2-(4- methoxy-N-(pyridine-3-YLMETHYL)PHENYLSULFONAMIDO)ACETAMIDE
Analyse Catalytic domain of stromelysin-1 in complex with N-hydroxy-2-(4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OHL
- Type
- protein
- Length
- 159 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stromelysin-1
- EC
- 3.4.24.17
- UniProt
- P08254
- Ligands
- OHL, CA, ZN, SO4
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stromelysin-1 (EC 3.4.24.17) | protein | 159 | 25% helix, 20% strand | P08254 |
Ligands and binding sites
- OHL · N-hydroxy-N~2~-[(4-methoxyphenyl)sulfonyl]-N~2~-(pyridin-4-ylmethyl)glycinamide · ligand · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.52 | 0.78 | 28 | OHL |
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 P08254
- Elsewhere: RCSB PDB 3OHL · PDBe 3OHL · UniProt P08254
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