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The crystal structure of upa complex with peptide inhibitor MH027 at PH7.4

Analyse The crystal structure of upa complex with peptide inhibitor MH027 at PH7.4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OY5
Type: protein
Length: 261 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 0.38

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	246	11% helix, 38% strand	P00749
P	MH027	protein	15	20% helix, 0% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 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	128	0.38	0.73	20	empty

Interfaces

1 interface between chains.

U–P · 772 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

3OY5 · The crystal structure of uPA complex with peptide inhibitor MH027 at pH7.4 · 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 3OY5 · PDBe 3OY5 · UniProt P00749

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