PDBsum entry 5l7f

Hydrolase

PDB id: 5l7f

Contents

Protein chains

158 a.a.

Ligands

EDO ×3

R47-6PJ

6PJ

R47

GOL

DMS

Metals

_ZN ×4

_CA ×6

_BR

Waters ×367

PDB id:

5l7f

Name:

Hydrolase

Title:

Crystal structure of mmp12 mutant k421a in complex with rxp470.1 conjugated with fluorophore cy5,5 in space group p21.

Structure:

Macrophage metalloelastase. Chain: a, b. Synonym: mme,macrophage elastase,hme,matrix metalloproteinase-12,mmp- 12. Engineered: yes. Mutation: yes. Other_details: fragment: catalytic domain (unp residues 106-263) mutations: f171d k241a

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: mmp12, hme. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.80Å R-factor: 0.177 R-free: 0.195

Authors:

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

Key ref:

T.Bordenave et al. (2016). Synthesis and in Vitro and in Vivo Evaluation of MMP-12 Selective Optical Probes. Bioconjug Chem, 27, 2407-2417. PubMed id: 27564088 DOI: 10.1021/acs.bioconjchem.6b00377

Date:

03-Jun-16 Release date: 14-Sep-16

Protein chains

P39900  (MMP12_HUMAN) -  Macrophage metalloelastase from Homo sapiens

Seq: 470 a.a.

Struc: 158 a.a.*

* PDB and UniProt seqs differ at 2 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.bioconjchem.6b00377

Bioconjug Chem 27:2407-2417 (2016)

PubMed id: 27564088

Synthesis and in Vitro and in Vivo Evaluation of MMP-12 Selective Optical Probes.

T.Bordenave, M.Helle, F.Beau, D.Georgiadis, L.Tepshi, M.Bernes, Y.Ye, L.Levenez, E.Poquet, H.Nozach, M.Razavian, J.Toczek, E.A.Stura, V.Dive, M.M.Sadeghi, L.Devel.

ABSTRACT

No abstract given.