Research workbench
Crystal structure of human microurokinase in complex with 2-amino-5- hydroxy-benzimidazole
Analyse Crystal structure of human microurokinase in complex with 2-amino-5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FV9
- Type
- protein
- Length
- 245 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Urokinase
- EC
- 3.4.21.73
- UniProt
- P00749
- Ligands
- 172, SO4
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Urokinase (EC 3.4.21.73) | protein | 245 | 10% helix, 40% strand | P00749 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.48 | 0.77 | 35 | SO4, 172 |
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 1FV9 · Crystal structure of human microurokinase in complex with 2-amino-5-hydroxy-benzimidazole · the same entry in another collection · chain A against A, TM-score 1.00
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 P00749
- Elsewhere: RCSB PDB 1FV9 · PDBe 1FV9 · UniProt P00749
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