Atomistry » Zinc » PDB 3eyl-3f7i » 3f16
Atomistry »
  Zinc »
    PDB 3eyl-3f7i »
      3f16 »

Zinc in PDB 3f16: Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1-Oxopropan-2-Yl)-4- Methoxybenzenesulfonamide

Enzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1-Oxopropan-2-Yl)-4- Methoxybenzenesulfonamide

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1-Oxopropan-2-Yl)-4- Methoxybenzenesulfonamide:
3.4.24.65;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1-Oxopropan-2-Yl)-4- Methoxybenzenesulfonamide, PDB code: 3f16 was solved by V.Calderone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.22 / 1.16
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 51.882, 60.366, 53.953, 90.00, 114.37, 90.00
R / Rfree (%) 16.1 / 18.2

Other elements in 3f16:

The structure of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1-Oxopropan-2-Yl)-4- Methoxybenzenesulfonamide also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1-Oxopropan-2-Yl)-4- Methoxybenzenesulfonamide (pdb code 3f16). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1-Oxopropan-2-Yl)-4- Methoxybenzenesulfonamide, PDB code: 3f16:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3f16

Go back to Zinc Binding Sites List in 3f16
Zinc binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1-Oxopropan-2-Yl)-4- Methoxybenzenesulfonamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1-Oxopropan-2-Yl)-4- Methoxybenzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn264

b:4.0
occ:1.00
 O3 A:HS30 1.9 9.8 1.0
NE2 A:HIS218 2.1 3.6 1.0
NE2 A:HIS228 2.1 3.9 1.0
O6 A:HS30 2.1 5.6 1.0
NE2 A:HIS222 2.1 3.6 1.0
C8 A:HS30 2.7 9.8 1.0
N1 A:HS30 2.8 7.8 1.0
CD2 A:HIS218 3.0 3.6 1.0
O A:HOH74 3.1 10.7 1.0
CE1 A:HIS228 3.1 3.8 1.0
CE1 A:HIS222 3.1 3.5 1.0
CE1 A:HIS218 3.1 5.0 1.0
CD2 A:HIS228 3.1 4.1 1.0
CD2 A:HIS222 3.1 3.2 1.0
O A:HOH17 4.1 5.8 1.0
OE1 A:GLU219 4.1 4.7 1.0
ND1 A:HIS218 4.2 4.9 1.0
ND1 A:HIS228 4.2 4.3 1.0
CG A:HIS218 4.2 3.5 1.0
ND1 A:HIS222 4.2 3.7 1.0
C9 A:HS30 4.2 12.1 1.0
CG A:HIS228 4.2 4.6 1.0
CG A:HIS222 4.3 3.3 1.0
O A:HOH64 4.5 10.2 1.0
O4 A:HS30 4.6 14.9 1.0
OE2 A:GLU219 4.8 4.5 1.0
C1 A:HS30 4.8 8.8 1.0
CD A:GLU219 4.8 3.9 1.0
C7 A:HS30 4.9 13.9 1.0
CE A:MET236 5.0 5.0 1.0

Zinc binding site 2 out of 2 in 3f16

Go back to Zinc Binding Sites List in 3f16
Zinc binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1-Oxopropan-2-Yl)-4- Methoxybenzenesulfonamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1-Oxopropan-2-Yl)-4- Methoxybenzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn265

b:6.1
occ:1.00
 OD1 A:ASP170 2.0 5.4 0.7
NE2 A:HIS168 2.0 5.3 1.0
NE2 A:HIS183 2.1 5.8 1.0
ND1 A:HIS196 2.1 5.1 1.0
CD2 A:HIS168 2.9 6.0 1.0
CG A:ASP170 3.0 7.3 0.7
CE1 A:HIS196 3.0 6.1 1.0
CE1 A:HIS183 3.0 6.6 1.0
CE1 A:HIS168 3.1 5.2 1.0
CD2 A:HIS183 3.1 5.7 1.0
CG A:HIS196 3.1 4.3 1.0
OD2 A:ASP170 3.2 5.4 0.7
CB A:HIS196 3.5 4.2 1.0
CG A:HIS168 4.1 6.6 1.0
ND1 A:HIS168 4.1 5.5 1.0
NE2 A:HIS196 4.1 5.5 1.0
ND1 A:HIS183 4.1 6.5 1.0
O A:HIS172 4.2 7.7 1.0
CD2 A:HIS196 4.2 4.7 1.0
CG A:HIS183 4.2 5.2 1.0
CE2 A:PHE185 4.3 11.5 1.0
CB A:ASP170 4.4 9.5 0.7
CZ A:PHE185 4.5 11.2 1.0
CZ A:PHE174 4.6 5.7 1.0
CE1 A:PHE174 4.7 5.5 1.0
CB A:HIS172 4.7 9.5 1.0
O A:HOH29 5.0 8.2 1.0
CA A:HIS196 5.0 3.5 1.0

Reference:

I.Bertini, V.Calderone, M.Fragai, A.Giachetti, M.Loconte, C.Luchinat, M.Maletta, C.Nativi, K.J.Yeo. Exploring the Subtleties of Drug-Receptor Interactions: the Case of Matrix Metalloproteinases. J.Am.Chem.Soc. V. 129 2466 2007.
ISSN: ISSN 0002-7863
PubMed: 17269766
DOI: 10.1021/JA065156Z
Page generated: Thu Oct 24 13:01:32 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy