Zinc in PDB 2ozr: MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid

The structure of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid, PDB code: 2ozr was solved by A.R.Johnson, A.G.Pavlovsky, D.F.Ortwine, F.Prior, C.-F.Man, D.A.Bornemeier, C.A.Banotai, W.T.Mueller, P.Mcconnell, C.H.Yan, V.Baragi, C.Lesch, W.H.Roark, J.J.Lie, V.Fasquelle, M.Wilson, D.Robertson, K.Datta, R.Guzman, H.-K.Han, R.D.Dyer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	161.836, 71.974, 138.130, 90.00, 124.59, 90.00
R / Rfree (%)	24.8 / 34

The structure of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid also contains other interesting chemical elements:

Calcium

(Ca)

24 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Zinc atom in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid (pdb code 2ozr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 16 binding sites of Zinc where determined in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid, PDB code: 2ozr:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 16 in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn4001 b:18.8 occ:1.00 NE2 A:HIS211 2.1 24.9 1.0 O A:HOH4024 2.1 26.7 1.0 NE2 A:HIS205 2.2 15.2 1.0 NE2 A:HIS201 2.2 14.6 1.0 O A:HOH4044 2.9 29.9 1.0 CE1 A:HIS211 3.0 25.8 1.0 CD2 A:HIS211 3.0 24.6 1.0 CD2 A:HIS205 3.1 16.3 1.0 CE1 A:HIS201 3.1 14.8 1.0 CE1 A:HIS205 3.2 16.3 1.0 CD2 A:HIS201 3.2 14.4 1.0 ND1 A:HIS211 4.1 25.6 1.0 OE2 A:GLU202 4.1 19.3 1.0 CG A:HIS211 4.1 24.8 1.0 CG A:HIS205 4.2 16.9 1.0 ND1 A:HIS201 4.3 14.4 1.0 ND1 A:HIS205 4.3 17.0 1.0 O A:HOH4027 4.3 27.4 1.0 CG A:HIS201 4.3 15.3 1.0 O A:HOH4014 4.4 24.6 1.0 OE1 A:GLU202 4.5 19.2 1.0 CD A:GLU202 4.6 17.7 1.0 O A:HOH4031 4.7 26.7 1.0 CE A:MET219 4.8 14.8 1.0 CA A:PRO221 5.0 24.2 1.0

Zinc binding site 2 out of 16 in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn4002 b:19.5 occ:1.00 OD2 A:ASP153 2.0 17.8 1.0 NE2 A:HIS151 2.0 13.8 1.0 ND1 A:HIS179 2.1 14.2 1.0 CE1 A:HIS166 2.2 23.3 1.0 NE2 A:HIS166 2.3 22.7 1.0 CD2 A:HIS151 2.8 15.6 1.0 CG A:ASP153 2.9 18.1 1.0 CE1 A:HIS179 3.1 15.1 1.0 CG A:HIS179 3.1 13.8 1.0 CE1 A:HIS151 3.1 14.0 1.0 OD1 A:ASP153 3.2 16.7 1.0 CB A:HIS179 3.4 14.4 1.0 ND1 A:HIS166 3.5 22.2 1.0 CD2 A:HIS166 3.6 22.0 1.0 CG A:HIS151 4.0 15.7 1.0 O A:TYR155 4.1 23.6 1.0 ND1 A:HIS151 4.1 14.3 1.0 NE2 A:HIS179 4.2 14.8 1.0 CG A:HIS166 4.2 21.7 1.0 CD2 A:HIS179 4.2 13.4 1.0 CB A:ASP153 4.3 19.2 1.0 CE1 A:PHE168 4.7 25.5 1.0 CB A:TYR155 4.7 24.7 1.0 CZ A:PHE157 4.7 19.7 1.0 CZ A:PHE168 4.8 25.1 1.0 CA A:HIS179 4.9 14.7 1.0 CE2 A:PHE157 4.9 18.4 1.0 C A:TYR155 4.9 23.8 1.0 O A:HOH4007 4.9 15.9 1.0

Zinc binding site 3 out of 16 in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn4006 b:20.0 occ:1.00 NE2 B:HIS211 2.1 24.1 1.0 NE2 B:HIS201 2.2 14.1 1.0 O B:HOH4058 2.2 37.0 1.0 NE2 B:HIS205 2.3 16.0 1.0 O B:HOH4022 2.4 25.6 1.0 CE1 B:HIS211 3.0 25.3 1.0 CD2 B:HIS201 3.1 14.8 1.0 CD2 B:HIS211 3.1 23.9 1.0 CD2 B:HIS205 3.2 15.1 1.0 CE1 B:HIS201 3.2 15.3 1.0 CE1 B:HIS205 3.3 16.9 1.0 OE2 B:GLU202 3.9 19.5 1.0 ND1 B:HIS211 4.1 25.3 1.0 CG B:HIS211 4.2 24.6 1.0 CG B:HIS201 4.3 15.6 1.0 ND1 B:HIS201 4.3 14.7 1.0 O B:HOH4113 4.3 29.5 1.0 ND1 B:HIS205 4.4 16.6 1.0 CG B:HIS205 4.4 16.2 1.0 O B:HOH4124 4.5 22.4 1.0 O B:HOH4023 4.5 17.9 1.0 CD B:GLU202 4.6 18.3 1.0 OE1 B:GLU202 4.8 19.2 1.0 CE B:MET219 4.8 15.5 1.0 O B:PRO221 4.9 25.0 1.0

Zinc binding site 4 out of 16 in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn4007 b:20.1 occ:1.00 NE2 B:HIS166 1.9 23.1 1.0 ND1 B:HIS179 2.0 13.7 1.0 OD2 B:ASP153 2.1 17.0 1.0 NE2 B:HIS151 2.2 15.0 1.0 CE1 B:HIS166 2.9 22.2 1.0 CD2 B:HIS151 2.9 15.1 1.0 CD2 B:HIS166 2.9 21.2 1.0 CE1 B:HIS179 3.0 15.4 1.0 CG B:ASP153 3.0 18.0 1.0 CG B:HIS179 3.1 13.3 1.0 OD1 B:ASP153 3.2 17.7 1.0 CE1 B:HIS151 3.3 14.7 1.0 CB B:HIS179 3.5 14.4 1.0 ND1 B:HIS166 4.0 21.6 1.0 CG B:HIS166 4.0 21.3 1.0 NE2 B:HIS179 4.1 14.9 1.0 CG B:HIS151 4.1 15.7 1.0 CD2 B:HIS179 4.2 13.7 1.0 ND1 B:HIS151 4.2 15.2 1.0 O B:TYR155 4.3 23.5 1.0 CB B:ASP153 4.4 19.0 1.0 CE1 B:PHE168 4.5 25.7 1.0 CZ B:PHE168 4.5 24.9 1.0 CB B:TYR155 4.8 24.9 1.0 CZ B:PHE157 4.8 19.7 1.0 CE2 B:PHE157 4.9 18.9 1.0 CA B:HIS179 5.0 14.3 1.0

Zinc binding site 5 out of 16 in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn4011 b:17.3 occ:1.00 NE2 C:HIS211 2.1 24.8 1.0 NE2 C:HIS201 2.1 15.0 1.0 NE2 C:HIS205 2.2 16.7 1.0 O C:HAE3001 2.3 30.0 1.0 N C:HAE3001 2.8 30.4 1.0 O2 C:HAE3001 2.9 31.1 1.0 CD2 C:HIS211 3.0 24.5 1.0 CD2 C:HIS205 3.0 16.4 1.0 CD2 C:HIS201 3.1 14.1 1.0 C2 C:HAE3001 3.1 30.9 1.0 CE1 C:HIS211 3.1 25.0 1.0 CE1 C:HIS201 3.1 14.7 1.0 CE1 C:HIS205 3.3 16.7 1.0 CG C:HIS211 4.2 24.5 1.0 ND1 C:HIS211 4.2 25.2 1.0 ND1 C:HIS201 4.2 14.3 1.0 CG C:HIS201 4.2 14.7 1.0 CG C:HIS205 4.2 17.0 1.0 ND1 C:HIS205 4.3 16.4 1.0 C1 C:HAE3001 4.3 28.8 1.0 OE2 C:GLU202 4.4 18.6 1.0 OE1 C:GLU202 4.6 19.1 1.0 CD C:GLU202 4.8 18.5 1.0 CE C:MET219 4.9 15.9 1.0 O C:PRO221 5.0 24.6 1.0

Zinc binding site 6 out of 16 in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn4012 b:17.7 occ:1.00 NE2 C:HIS166 2.0 23.0 1.0 OD2 C:ASP153 2.0 18.4 1.0 NE2 C:HIS151 2.1 12.8 1.0 ND1 C:HIS179 2.1 15.9 1.0 CE1 C:HIS166 2.9 23.2 1.0 CD2 C:HIS151 3.0 14.2 1.0 CG C:ASP153 3.0 19.1 1.0 CE1 C:HIS179 3.1 16.1 1.0 CD2 C:HIS166 3.1 22.3 1.0 CE1 C:HIS151 3.1 14.1 1.0 CG C:HIS179 3.1 14.8 1.0 OD1 C:ASP153 3.3 17.9 1.0 CB C:HIS179 3.4 14.3 1.0 ND1 C:HIS166 4.0 22.5 1.0 O C:TYR155 4.1 23.5 1.0 CG C:HIS151 4.1 15.5 1.0 CG C:HIS166 4.2 21.4 1.0 ND1 C:HIS151 4.2 14.7 1.0 NE2 C:HIS179 4.2 15.1 1.0 CD2 C:HIS179 4.3 14.3 1.0 CB C:ASP153 4.4 18.9 1.0 CE1 C:PHE168 4.5 24.1 1.0 CZ C:PHE168 4.5 24.7 1.0 CZ C:PHE157 4.7 18.4 1.0 CE2 C:PHE157 4.7 18.4 1.0 CB C:TYR155 4.8 24.3 1.0 CA C:HIS179 4.9 14.4 1.0 C C:TYR155 5.0 23.4 1.0

Zinc binding site 7 out of 16 in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn4016 b:16.9 occ:1.00 NE2 D:HIS211 2.1 23.8 1.0 NE2 D:HIS201 2.2 16.0 1.0 O2 D:HAE3002 2.3 32.9 1.0 NE2 D:HIS205 2.3 16.1 1.0 C2 D:HAE3002 2.6 34.3 1.0 O D:HAE3002 2.8 33.8 1.0 N D:HAE3002 2.8 34.2 1.0 CD2 D:HIS211 3.0 24.0 1.0 CE1 D:HIS211 3.0 24.4 1.0 CD2 D:HIS201 3.0 15.2 1.0 CD2 D:HIS205 3.2 16.4 1.0 CE1 D:HIS201 3.2 15.3 1.0 CE1 D:HIS205 3.4 15.7 1.0 C1 D:HAE3002 3.6 34.5 1.0 ND1 D:HIS211 4.1 24.6 1.0 CG D:HIS211 4.1 24.5 1.0 CG D:HIS201 4.2 15.7 1.0 ND1 D:HIS201 4.3 14.9 1.0 OE1 D:GLU202 4.3 19.1 1.0 CG D:HIS205 4.4 16.2 1.0 OE2 D:GLU202 4.4 16.8 1.0 ND1 D:HIS205 4.4 15.0 1.0 O D:HOH4153 4.4 22.4 1.0 O D:HOH4156 4.6 23.0 1.0 CD D:GLU202 4.7 17.8 1.0 CE D:MET219 4.7 15.6 1.0 O D:PRO221 5.0 24.2 1.0

Zinc binding site 8 out of 16 in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn4017 b:18.1 occ:1.00 ND1 D:HIS179 2.0 14.7 1.0 OD2 D:ASP153 2.0 19.0 1.0 NE2 D:HIS166 2.0 22.3 1.0 NE2 D:HIS151 2.1 11.8 1.0 CE1 D:HIS166 2.8 22.7 1.0 CD2 D:HIS151 2.9 14.0 1.0 CG D:ASP153 2.9 19.0 1.0 CE1 D:HIS179 2.9 15.9 1.0 CG D:HIS179 3.0 14.9 1.0 CD2 D:HIS166 3.2 21.7 1.0 OD1 D:ASP153 3.2 17.1 1.0 CE1 D:HIS151 3.3 14.0 1.0 CB D:HIS179 3.4 14.8 1.0 ND1 D:HIS166 4.0 21.1 1.0 NE2 D:HIS179 4.1 15.1 1.0 CD2 D:HIS179 4.1 14.3 1.0 O D:TYR155 4.2 23.9 1.0 CG D:HIS151 4.2 15.4 1.0 CG D:HIS166 4.2 20.6 1.0 ND1 D:HIS151 4.3 14.7 1.0 CB D:ASP153 4.3 19.1 1.0 CE1 D:PHE168 4.6 25.1 1.0 CZ D:PHE157 4.7 18.6 1.0 CZ D:PHE168 4.7 25.0 1.0 CE2 D:PHE157 4.7 19.1 1.0 CB D:TYR155 4.9 24.6 1.0 CA D:HIS179 4.9 14.8 1.0 C D:TYR155 5.0 23.8 1.0

Zinc binding site 9 out of 16 in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn4021 b:34.1 occ:1.00 NE2 E:HIS205 1.9 17.5 1.0 O2 E:HAE3003 2.0 39.1 1.0 NE2 E:HIS201 2.3 16.2 1.0 NE2 E:HIS211 2.4 27.0 1.0 O E:HAE3003 2.5 41.5 1.0 C2 E:HAE3003 2.7 41.5 1.0 CD2 E:HIS205 2.8 18.1 1.0 CD2 E:HIS211 2.9 26.3 1.0 N E:HAE3003 3.0 41.4 1.0 CE1 E:HIS201 3.0 16.6 1.0 CE1 E:HIS205 3.0 18.1 1.0 CD2 E:HIS201 3.4 16.3 1.0 CE1 E:HIS211 3.6 27.1 1.0 CG E:HIS205 4.0 18.4 1.0 ND1 E:HIS205 4.1 18.5 1.0 ND1 E:HIS201 4.1 17.5 1.0 C1 E:HAE3003 4.1 41.9 1.0 CG E:HIS211 4.2 26.5 1.0 O E:HOH4068 4.3 30.9 1.0 CG E:HIS201 4.3 17.3 1.0 ND1 E:HIS211 4.5 27.5 1.0 OE2 E:GLU202 4.7 19.7 1.0 OE1 E:GLU202 4.7 20.2 1.0 CE E:MET219 4.8 15.6 1.0 CD E:GLU202 5.0 18.3 1.0

Zinc binding site 10 out of 16 in the MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of MMP13 Catalytic Domain Complexed with 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2H)-Yl]Methyl}Benzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn4022 b:23.8 occ:1.00 OD2 E:ASP153 2.0 17.7 1.0 NE2 E:HIS151 2.0 15.3 1.0 NE2 E:HIS166 2.1 23.8 1.0 ND1 E:HIS179 2.2 15.3 1.0 CD2 E:HIS151 2.9 14.7 1.0 CG E:ASP153 2.9 18.1 1.0 CD2 E:HIS166 3.1 22.8 1.0 CE1 E:HIS151 3.1 15.3 1.0 CE1 E:HIS166 3.1 23.5 1.0 CG E:HIS179 3.1 14.8 1.0 CE1 E:HIS179 3.2 16.2 1.0 OD1 E:ASP153 3.2 16.3 1.0 CB E:HIS179 3.4 15.4 1.0 CG E:HIS151 4.1 16.1 1.0 O E:TYR155 4.1 24.7 1.0 ND1 E:HIS151 4.1 15.7 1.0 ND1 E:HIS166 4.2 23.1 1.0 CG E:HIS166 4.2 22.8 1.0 CD2 E:HIS179 4.3 15.5 1.0 NE2 E:HIS179 4.3 15.3 1.0 CB E:ASP153 4.3 19.3 1.0 CE2 E:PHE157 4.5 18.8 1.0 CZ E:PHE157 4.5 18.7 1.0 CE1 E:PHE168 4.8 25.2 1.0 O E:HOH4104 4.8 15.0 1.0 CA E:HIS179 4.8 15.5 1.0 CZ E:PHE168 4.9 25.9 1.0

A.R.Johnson, A.G.Pavlovsky, D.F.Ortwine, F.Prior, C.F.Man, D.A.Bornemeier, C.A.Banotai, W.T.Mueller, P.Mcconnell, C.Yan, V.Baragi, C.Lesch, W.H.Roark, M.Wilson, K.Datta, R.Guzman, H.K.Han, R.D.Dyer. Discovery and Characterization of A Novel Inhibitor of Matrix Metalloprotease-13 That Reduces Cartilage Damage in Vivo Without Joint Fibroplasia Side Effects. J.Biol.Chem. V. 282 27781 2007.
ISSN: ISSN 0021-9258
PubMed: 17623656
DOI: 10.1074/JBC.M703286200