› 1eak

X-ray diffraction
2.66Å resolution

Catalytic domain of proMMP-2 E404Q mutant

Released:
DOI: 10.2210/pdb1eak/pdb
PDB entry 1eak coloured by chain, front view.
PDB entry 1eak coloured by chain, side view.
PDB entry 1eak coloured by chain, top view.
Source organisms:
Entry authors: Bergmann U, Tuuttila A, Tryggvason K, Morgunova E

Function and Biology Details

Reaction catalysed: 
Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140078 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
72 kDa type IV collagenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 421 amino acids
Theoretical weight: 47.3 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P08253 (Residues: 32-452; Coverage: 67%)
Gene names: CLG4A, MMP2
Sequence domains:
Structure domains:
INHIBITOR PEPTIDE Chains: P, R
Molecule details ›
Chains: P, R
Length: 8 amino acids
Theoretical weight: 623 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand SO4 6 x SO4
Ligand ZN 8 x ZN
Ligand CA 8 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE D2AM
Spacegroup: P212121
Unit cell:
a: 117.67Å b: 166.15Å c: 170.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.271 0.271 0.303
Expression systems:
  • Trichoplusia ni
  • Not provided

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