PDBe 2e2d

X-ray diffraction
2Å resolution

Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Collagenase 3 Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P45452 (Residues: 104-268; Coverage: 37%)
Gene name: MMP13
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Metalloproteinase inhibitor 2 Chain: C
Molecule details ›
Chain: C
Length: 180 amino acids
Theoretical weight: 20.19 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P16368 (Residues: 28-206; Coverage: 92%)
Gene name: TIMP2
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P65
Unit cell:
a: 72.526Å b: 72.526Å c: 181.375Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.2 0.231
Expression system: Escherichia coli