› 3rtt

X-ray diffraction
1.82Å resolution

Human MMP-12 catalytic domain in complex with*(R)-N*-Hydroxy-1-(phenethylsulfonyl)pyrrolidine-2-carboxamide

Released:
DOI: 10.2210/pdb3rtt/pdb
PDB entry 3rtt coloured by chain, front view.
PDB entry 3rtt coloured by chain, side view.
PDB entry 3rtt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Contribution of ligand free energy of solvation to design new potent MMPs inhibitors.
Mordini A, Mori M, Massaro A, Calderone V, Fragai M, Luchinat C
J. Med. Chem. (2012)

Function and Biology Details

Reaction catalysed: 
Hydrolysis of soluble and insoluble elastin (1). Specific cleavages are also produced at -Ala(14)-|-Leu- and -Tyr(16)-|-Leu- in the B chain of insulin (2).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153971 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Macrophage metalloelastase Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P39900 (Residues: 106-263; Coverage: 35%)
Gene names: HME, MMP12
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 3 x CA
Ligand KLH 1 x KLH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: C2
Unit cell:
a: 51.487Å b: 60.431Å c: 54.207Å
α: 90° β: 115.21° γ: 90°
R-values:
R R work R free
0.242 0.234 0.317
Expression system: Escherichia coli

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