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Zinc in PDB 2z2d: Solution Structure of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed with A Gamma-Keto Butanoic Acid Inhibitor

Enzymatic activity of Solution Structure of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed with A Gamma-Keto Butanoic Acid Inhibitor

All present enzymatic activity of Solution Structure of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed with A Gamma-Keto Butanoic Acid Inhibitor:
3.4.24.65;

Other elements in 2z2d:

The structure of Solution Structure of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed with A Gamma-Keto Butanoic Acid Inhibitor also contains other interesting chemical elements:

Chlorine (Cl) 15 atoms
Calcium (Ca) 45 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed with A Gamma-Keto Butanoic Acid Inhibitor (pdb code 2z2d). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed with A Gamma-Keto Butanoic Acid Inhibitor, PDB code: 2z2d:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2z2d

Go back to Zinc Binding Sites List in 2z2d
Zinc binding site 1 out of 2 in the Solution Structure of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed with A Gamma-Keto Butanoic Acid Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed with A Gamma-Keto Butanoic Acid Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn264

b:2.0
occ:1.00
NE2 A:HIS218 1.9 -0.6 1.0
NE2 A:HIS228 2.0 -0.6 1.0
NE2 A:HIS222 2.0 -0.6 1.0
O A:MET236 2.7 -0.6 1.0
CE1 A:HIS218 2.9 0.0 1.0
CD2 A:HIS222 3.0 0.1 1.0
HE2 A:MET236 3.0 0.0 1.0
CD2 A:HIS218 3.0 0.1 1.0
CE1 A:HIS228 3.0 0.0 1.0
CE1 A:HIS222 3.0 0.0 1.0
CD2 A:HIS228 3.1 0.1 1.0
HE1 A:HIS218 3.1 0.1 1.0
HD2 A:HIS222 3.2 0.1 1.0
HD2 A:HIS218 3.3 0.1 1.0
HE1 A:HIS228 3.3 0.1 1.0
HD2 A:HIS228 3.3 0.1 1.0
HE1 A:HIS222 3.4 0.1 1.0
C A:MET236 3.8 0.6 1.0
O4 A:HSI269 3.8 -0.6 1.0
HA A:MET236 4.0 0.0 1.0
ND1 A:HIS218 4.0 0.0 1.0
CG A:HIS222 4.1 -0.3 1.0
CE A:MET236 4.1 0.2 1.0
ND1 A:HIS222 4.1 0.0 1.0
HB3 A:MET236 4.1 0.0 1.0
C3 A:HSI269 4.1 0.7 1.0
CG A:HIS218 4.1 -0.3 1.0
ND1 A:HIS228 4.2 0.0 1.0
CG A:HIS228 4.3 -0.3 1.0
HA A:PRO238 4.3 0.0 1.0
H51 A:HSI269 4.3 0.0 1.0
CA A:MET236 4.4 0.4 1.0
HE1 A:MET236 4.4 0.0 1.0
HO1 A:HSI269 4.5 0.5 1.0
HE3 A:MET236 4.6 0.0 1.0
O1 A:HSI269 4.6 -0.7 1.0
CB A:MET236 4.7 0.0 1.0
C5 A:HSI269 4.7 0.1 1.0
O A:PHE237 4.7 -0.6 1.0
H52 A:HSI269 4.7 0.0 1.0
HD3 A:PRO238 4.7 0.0 1.0
C A:PHE237 4.8 0.6 1.0
HD1 A:HIS218 4.9 0.3 1.0
N A:PHE237 4.9 -0.7 1.0
N A:PRO238 5.0 -0.7 1.0
HG2 A:MET236 5.0 0.0 1.0

Zinc binding site 2 out of 2 in 2z2d

Go back to Zinc Binding Sites List in 2z2d
Zinc binding site 2 out of 2 in the Solution Structure of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed with A Gamma-Keto Butanoic Acid Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed with A Gamma-Keto Butanoic Acid Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn265

b:2.0
occ:1.00
ND1 A:HIS196 1.8 -1.3 1.0
OD1 A:ASP170 2.0 -0.9 1.0
NE2 A:HIS183 2.1 -0.6 1.0
OD2 A:ASP170 2.3 -0.9 1.0
NE2 A:HIS168 2.4 -0.6 1.0
CG A:ASP170 2.5 0.9 1.0
HB3 A:HIS196 2.7 0.0 1.0
CG A:HIS196 2.8 -0.0 1.0
CE1 A:HIS196 2.8 0.3 1.0
CD2 A:HIS183 2.9 0.1 1.0
CE1 A:HIS183 2.9 0.0 1.0
HE1 A:HIS196 3.0 0.1 1.0
HD2 A:HIS168 3.1 0.1 1.0
CD2 A:HIS168 3.1 0.1 1.0
HD2 A:HIS183 3.1 0.1 1.0
HE1 A:HIS183 3.2 0.1 1.0
CB A:HIS196 3.3 0.2 1.0
CE1 A:HIS168 3.5 0.0 1.0
ND1 A:HIS183 3.8 0.0 1.0
NE2 A:HIS196 3.9 0.1 1.0
CD2 A:HIS196 3.9 0.1 1.0
HB2 A:HIS196 3.9 0.0 1.0
CG A:HIS183 3.9 -0.3 1.0
HE1 A:HIS168 3.9 0.1 1.0
CB A:ASP170 3.9 -0.1 1.0
H A:ASP170 4.2 0.4 1.0
HZ A:PHE174 4.2 0.1 1.0
HB2 A:ASP170 4.4 0.0 1.0
CG A:HIS168 4.4 -0.3 1.0
HE1 A:PHE185 4.4 0.1 1.0
CA A:HIS196 4.5 0.4 1.0
O A:HIS196 4.5 -0.6 1.0
ND1 A:HIS168 4.5 0.0 1.0
N A:ASP170 4.5 -0.7 1.0
CA A:ASP170 4.6 0.4 1.0
HB3 A:ASP170 4.6 0.0 1.0
HA A:ASP170 4.6 0.0 1.0
HE2 A:PHE174 4.7 0.1 1.0
HD1 A:HIS183 4.7 0.3 1.0
CZ A:PHE174 4.7 -0.1 1.0
HE2 A:HIS196 4.8 0.4 1.0
H A:HIS196 4.8 0.4 1.0
C A:HIS196 4.9 0.6 1.0
HD2 A:HIS196 4.9 0.1 1.0
N A:HIS196 4.9 -0.7 1.0
C A:GLY169 5.0 0.6 1.0
CE2 A:PHE174 5.0 -0.1 1.0

Reference:

X.Zheng, L.Ou. Solution Structure of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed with A Gamma-Keto Butanoic Acid Inhibitor To Be Published.
Page generated: Wed Dec 16 04:04:12 2020

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