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Zinc in PDB 3f15: Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (S)-N-(2,3-Dihydroxypropyl)-4-Methoxy-N-(2- Nitroso-2-Oxoethyl)Benzenesulfonamide

Enzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (S)-N-(2,3-Dihydroxypropyl)-4-Methoxy-N-(2- Nitroso-2-Oxoethyl)Benzenesulfonamide

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (S)-N-(2,3-Dihydroxypropyl)-4-Methoxy-N-(2- Nitroso-2-Oxoethyl)Benzenesulfonamide:
3.4.24.65;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (S)-N-(2,3-Dihydroxypropyl)-4-Methoxy-N-(2- Nitroso-2-Oxoethyl)Benzenesulfonamide, PDB code: 3f15 was solved by V.Calderone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.45 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 51.557, 60.472, 53.859, 90.00, 114.55, 90.00
R / Rfree (%) 17.1 / 19

Other elements in 3f15:

The structure of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (S)-N-(2,3-Dihydroxypropyl)-4-Methoxy-N-(2- Nitroso-2-Oxoethyl)Benzenesulfonamide 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 (S)-N-(2,3-Dihydroxypropyl)-4-Methoxy-N-(2- Nitroso-2-Oxoethyl)Benzenesulfonamide (pdb code 3f15). 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 (S)-N-(2,3-Dihydroxypropyl)-4-Methoxy-N-(2- Nitroso-2-Oxoethyl)Benzenesulfonamide, PDB code: 3f15:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3f15

Go back to Zinc Binding Sites List in 3f15
Zinc binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (S)-N-(2,3-Dihydroxypropyl)-4-Methoxy-N-(2- Nitroso-2-Oxoethyl)Benzenesulfonamide


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 (S)-N-(2,3-Dihydroxypropyl)-4-Methoxy-N-(2- Nitroso-2-Oxoethyl)Benzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn264

b:6.6
occ:1.00
 NE2 A:HIS228 2.0 8.0 1.0
NE2 A:HIS218 2.1 4.7 1.0
NE2 A:HIS222 2.1 3.7 1.0
O7 A:HS10 2.1 8.2 1.0
O5 A:HS10 2.1 6.1 1.0
C9 A:HS10 2.9 8.7 1.0
N2 A:HS10 2.9 6.9 1.0
CD2 A:HIS218 3.0 4.4 1.0
CD2 A:HIS228 3.0 7.3 1.0
CE1 A:HIS228 3.0 6.7 1.0
CD2 A:HIS222 3.1 3.5 1.0
CE1 A:HIS218 3.1 4.6 1.0
CE1 A:HIS222 3.1 3.5 1.0
O A:HOH17 4.1 8.6 1.0
OE1 A:GLU219 4.1 6.4 1.0
ND1 A:HIS228 4.1 6.2 1.0
CG A:HIS218 4.2 3.8 1.0
CG A:HIS228 4.2 6.6 1.0
ND1 A:HIS218 4.2 5.6 1.0
ND1 A:HIS222 4.2 4.3 1.0
CG A:HIS222 4.3 4.1 1.0
C11 A:HS10 4.4 10.8 1.0
N1 A:HS10 4.6 11.9 1.0
O A:HOH72 4.7 18.8 1.0
C5 A:HS10 4.8 9.4 1.0
CE A:MET236 4.9 8.9 1.0
CD A:GLU219 4.9 6.8 1.0

Zinc binding site 2 out of 2 in 3f15

Go back to Zinc Binding Sites List in 3f15
Zinc binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor (S)-N-(2,3-Dihydroxypropyl)-4-Methoxy-N-(2- Nitroso-2-Oxoethyl)Benzenesulfonamide


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 (S)-N-(2,3-Dihydroxypropyl)-4-Methoxy-N-(2- Nitroso-2-Oxoethyl)Benzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn265

b:9.7
occ:1.00
 NE2 A:HIS183 1.9 13.0 1.0
OD1 A:ASP170 1.9 6.8 0.7
NE2 A:HIS168 2.1 7.8 1.0
ND1 A:HIS196 2.1 6.5 1.0
CE1 A:HIS183 2.6 16.2 1.0
CG A:ASP170 2.9 11.3 0.7
CD2 A:HIS168 2.9 8.1 1.0
CE1 A:HIS196 3.1 5.2 1.0
CD2 A:HIS183 3.1 15.4 1.0
CG A:HIS196 3.1 5.6 1.0
CE1 A:HIS168 3.2 8.1 1.0
OD2 A:ASP170 3.2 7.0 0.7
CB A:HIS196 3.5 5.1 1.0
ND1 A:HIS183 3.8 15.6 1.0
CG A:HIS183 4.1 10.3 1.0
CG A:HIS168 4.1 8.8 1.0
O A:HIS172 4.1 13.2 1.0
ND1 A:HIS168 4.2 7.8 1.0
CB A:ASP170 4.2 13.3 0.7
NE2 A:HIS196 4.2 6.3 1.0
CD2 A:HIS196 4.3 5.1 1.0
CE2 A:PHE185 4.4 14.4 1.0
CB A:HIS172 4.5 16.2 1.0
CZ A:PHE185 4.6 14.3 1.0
CZ A:PHE174 4.6 5.8 1.0
CE1 A:PHE174 4.7 8.7 1.0
CA A:HIS196 5.0 5.1 1.0
C A:HIS172 5.0 13.5 1.0
O A:HOH52 5.0 9.0 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

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