Research workbench
The crystal structure of upa complex with peptide inhibitor MH027 at PH4.6
Analyse The crystal structure of upa complex with peptide inhibitor MH027 at PH4.6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OX7
- Type
- protein
- Length
- 259 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Urokinase-type plasminogen activator; MH027
- EC
- 3.4.21.73
- UniProt
- P00749
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| U | Urokinase-type plasminogen activator (EC 3.4.21.73) | protein | 245 | 11% helix, 38% strand | P00749 |
| P | MH027 | protein | 14 | 21% helix, 0% strand | — |
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 | 139 | 0.40 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- U–P · 714 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 3OX7 · The crystal structure of uPA complex with peptide inhibitor MH027 at pH4.6 · the same entry in another collection · chain U against U, 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 3OX7 · PDBe 3OX7 · UniProt P00749
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