PDBsum entry 5d3c

Hydrolase

PDB id: 5d3c

Contents

Protein chain

159 a.a.

Ligands

56O

Metals

_ZN ×2

_CA ×3

Waters ×274

PDB id:

5d3c

Name:

Hydrolase

Title:

Crystal structure of a double mutant catalytic domain of human mmp12 in complex with an hydroxamate analogue of rxp470

Structure:

Macrophage metalloelastase. Chain: a. Fragment: unp residues 106-263. Synonym: mme,macrophage elastase,hme,matrix metalloproteinase-12,mmp- 12. Engineered: yes. Mutation: yes. Other_details: mmp12 f171d k141a mutant for calorimetric studies catalytic domain (unp residues 106-263)

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: mmp12, hme. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.31Å R-factor: 0.155 R-free: 0.191

Authors:

C.Rouanet-Mehouas,L.Devel,V.Dive,E.A.Stura

Key ref:

C.Rouanet-Mehouas et al. (2017). Zinc-Metalloproteinase Inhibitors: Evaluation of the Complex Role Played by the Zinc-Binding Group on Potency and Selectivity. J Med Chem, 60, 403-414. PubMed id: 27996256 DOI: 10.1021/acs.jmedchem.6b01420

Date:

06-Aug-15 Release date: 17-Aug-16

Protein chain

P39900  (MMP12_HUMAN) -  Macrophage metalloelastase from Homo sapiens

Seq: 470 a.a.

Struc: 159 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.24.65 - macrophage elastase.
• Reaction: Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.
• Cofactor: Ca(2+); Zn(2+)

DOI no: 10.1021/acs.jmedchem.6b01420

J Med Chem 60:403-414 (2017)

PubMed id: 27996256

Zinc-Metalloproteinase Inhibitors: Evaluation of the Complex Role Played by the Zinc-Binding Group on Potency and Selectivity.

C.Rouanet-Mehouas, B.Czarny, F.Beau, E.Cassar-Lajeunesse, E.A.Stura, V.Dive, L.Devel.

ABSTRACT

No abstract given.