3bn9

X-ray diffraction
2.17Å resolution

Crystal Structure of MT-SP1 in complex with Fab Inhibitor E2

Released:

Function and Biology Details

Reaction catalysed:
Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-208524 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Suppressor of tumorigenicity 14 protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 241 amino acids
Theoretical weight: 26.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y5Y6 (Residues: 615-855; Coverage: 28%)
Gene names: PRSS14, SNC19, ST14, TADG15
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
E2 Fab Light Chain Chains: C, E
Molecule details ›
Chains: C, E
Length: 214 amino acids
Theoretical weight: 23.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins
Immunoglobulin heavy variable 3-23 Chains: D, F
Molecule details ›
Chains: D, F
Length: 257 amino acids
Theoretical weight: 27.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01764 (Residues: 20-117; Coverage: 100%)
Gene name: IGHV3-23
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 48.625Å b: 163.279Å c: 201.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.223 0.267
Expression system: Escherichia coli