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Crystal structure of upa in complex with cleaved camostat

Analyse Crystal structure of upa in complex with cleaved camostat in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DZD
Type
protein
Length
245 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Urokinase-type plasminogen activator
EC
3.4.21.73
UniProt
P00749
Ligands
GBS
Pockets
1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
UUrokinase-type plasminogen activator (EC 3.4.21.73)protein24511% helix, 39% strandP00749

Ligands and binding sites

  • GBS · 4-guanidinobenzoic acid · ligand · chains U
  • PGE · Triethylene glycol · additive · 2 copies · chains U

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11970.490.7635GBS

Modifications

Observed in the structure: 5 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

  • 7DZD · Crystal structure of uPA in complex with cleaved camostat · the same entry in another collection · chain U against U, TM-score 1.00

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