› 2r0l

X-ray diffraction
2.2Å resolution

Short Form HGFA with Inhibitory Fab75

Released:
DOI: 10.2210/pdb2r0l/pdb
PDB entry 2r0l coloured by chain, front view.
PDB entry 2r0l coloured by chain, side view.
PDB entry 2r0l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insight into distinct mechanisms of protease inhibition by antibodies.
Wu Y, Eigenbrot C, Liang WC, Stawicki S, Shia S, Fan B, Ganesan R, Lipari MT, Kirchhofer D
Proc Natl Acad Sci U S A 104 19784-9 (2007)
PMID: 18077410

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-211909 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (5 distinct):
antibody light chain Chain: L
Molecule details ›
Chain: L
Length: 214 amino acids
Theoretical weight: 23.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins
antibody heavy chain, Fab portion only Chain: H
Molecule details ›
Chain: H
Length: 220 amino acids
Theoretical weight: 23.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins
Hepatocyte growth factor activator long chain Chain: A
Molecule details ›
Chain: A
Length: 248 amino acids
Theoretical weight: 26.94 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q04756 (Residues: 408-655; Coverage: 40%)
Gene name: HGFAC
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Hepatocyte growth factor activator short chain Chain: B
Molecule details ›
Chain: B
Length: 35 amino acids
Theoretical weight: 3.96 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q04756 (Residues: 373-407; Coverage: 6%)
Gene name: HGFAC

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P1
Unit cell:
a: 38.82Å b: 48.23Å c: 97.05Å
α: 98.39° β: 96.24° γ: 100.77°
R-values:
R R work R free
0.195 0.193 0.248
Expression systems:
  • Escherichia coli
  • Spodoptera frugiperda

Quick links

Citations

10 review citations

Targeting MET in cancer: rationale and progress.
Gherardi et al. (2012)
9 more

8 mentions without citation

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.
Goettig P. (2016)
7 more