› 4x1p

X-ray diffraction
1.6Å resolution

The crystal structure of mupain-1-17 in complex with murinised human uPA at pH4.6

Released:
DOI: 10.2210/pdb4x1p/pdb
PDB entry 4x1p coloured by chain, front view.
PDB entry 4x1p coloured by chain, side view.
PDB entry 4x1p coloured by chain, top view.
Source organisms:
Primary publication:
Distinctive binding modes and inhibitory mechanisms of two peptidic inhibitors of urokinase-type plasminogen activator with isomeric P1 residues.
Jiang L, Zhao B, Xu P, Sørensen HP, Jensen JK, Christensen A, Hosseini M, Nielsen NC, Jensen KJ, Andreasen PA, Huang M
Int J Biochem Cell Biol 62 88-92 (2015)
PMID: 25744057

Function and Biology Details

Reaction catalysed: 
Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133277 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Urokinase-type plasminogen activator chain B Chain: U
Molecule details ›
Chain: U
Length: 247 amino acids
Theoretical weight: 27.87 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P00749 (Residues: 179-425; Coverage: 60%)
Gene name: PLAU
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
MUPAIN-1-17 Chain: P
Molecule details ›
Chain: P
Length: 10 amino acids
Theoretical weight: 1.11 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand PGE 2 x PGE
Ligand MRZ 1 x MRZ
1 modified residue:
Ligand DAL 1 x DAL

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: R3
Unit cell:
a: 121.082Å b: 121.082Å c: 43.242Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.181 0.211
Expression systems:
  • Komagataella pastoris
  • Not provided

Quick links

Citations

1 citations in other articles

Selection of High-Affinity Peptidic Serine Protease Inhibitors with Increased Binding Entropy from a Back-Flip Library of Peptide-Protease Fusions.
Sørensen et al. (2015)