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The crystal structure of human urokinase-type plasminogen activator catalytic domain

Analyse The crystal structure of human urokinase-type plasminogen activator catalytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4DVA
Type
protein
Length
246 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
SO4
Pockets
1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
UUrokinase-type plasminogen activator (EC 3.4.21.73)protein24611% helix, 38% strandP00749

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains U
  • P6G · Hexaethylene 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
11490.440.7632SO4

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 4DVA · The crystal structure of human urokinase-type plasminogen activator catalytic domain · the same entry in another collection · chain U against U, TM-score 1.00

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