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The crystal structure of uPA in complex with HMA-55F

Analyse The crystal structure of uPA in complex with HMA-55F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AG7
Type: protein
Length: 245 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.9
Source: Homo sapiens
Molecule: Urokinase-type plasminogen activator
EC: 3.4.21.73
UniProt: P00749
Ligands: H55
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · resolution 1.9 · 1 distinct chain · 11% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
U	Urokinase-type plasminogen activator (EC 3.4.21.73)	protein	245	11% helix, 39% strand	P00749

Ligands and binding sites

H55 · 3,5-diamino-N-carbamimidoyl-6-(1-methyl-1H-pyrazol-4-yl)pyrazine-2-carboxamide · ligand · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	163	0.43	0.74	32	H55

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

6AG7 · The crystal structure of upa in complex with hma-55F · 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 6AG7 · PDBe 6AG7 · UniProt P00749

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