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Zinc in PDB 1ums: Stromelysin-1 Catalytic Domain with Hydrophobic Inhibitor Bound, pH 7.0, 32OC, 20 Mm CACL2, 15% Acetonitrile; uc(Nmr) Ensemble of 20 Structures

Enzymatic activity of Stromelysin-1 Catalytic Domain with Hydrophobic Inhibitor Bound, pH 7.0, 32OC, 20 Mm CACL2, 15% Acetonitrile; uc(Nmr) Ensemble of 20 Structures

All present enzymatic activity of Stromelysin-1 Catalytic Domain with Hydrophobic Inhibitor Bound, pH 7.0, 32OC, 20 Mm CACL2, 15% Acetonitrile; uc(Nmr) Ensemble of 20 Structures:
3.4.24.17;

Other elements in 1ums:

The structure of Stromelysin-1 Catalytic Domain with Hydrophobic Inhibitor Bound, pH 7.0, 32OC, 20 Mm CACL2, 15% Acetonitrile; uc(Nmr) Ensemble of 20 Structures also contains other interesting chemical elements:

Calcium (Ca) 20 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Stromelysin-1 Catalytic Domain with Hydrophobic Inhibitor Bound, pH 7.0, 32OC, 20 Mm CACL2, 15% Acetonitrile; uc(Nmr) Ensemble of 20 Structures (pdb code 1ums). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Stromelysin-1 Catalytic Domain with Hydrophobic Inhibitor Bound, pH 7.0, 32OC, 20 Mm CACL2, 15% Acetonitrile; uc(Nmr) Ensemble of 20 Structures, PDB code: 1ums:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1ums

Go back to Zinc Binding Sites List in 1ums
Zinc binding site 1 out of 2 in the Stromelysin-1 Catalytic Domain with Hydrophobic Inhibitor Bound, pH 7.0, 32OC, 20 Mm CACL2, 15% Acetonitrile; uc(Nmr) Ensemble of 20 Structures


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Stromelysin-1 Catalytic Domain with Hydrophobic Inhibitor Bound, pH 7.0, 32OC, 20 Mm CACL2, 15% Acetonitrile; uc(Nmr) Ensemble of 20 Structures within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:0.0
occ:1.00
 O2 A:HAE261 2.3 0.0 1.0
O A:HAE261 2.3 0.0 1.0
NE2 A:HIS201 2.3 0.0 1.0
NE2 A:HIS211 2.3 0.0 1.0
NE2 A:HIS205 2.3 0.0 1.0
HH A:TYR155 2.4 0.0 1.0
HE1 A:HIS205 2.8 0.0 1.0
CE1 A:HIS205 2.9 0.0 1.0
CD2 A:HIS211 2.9 0.0 1.0
CD2 A:HIS201 3.0 0.0 1.0
HD2 A:HIS201 3.0 0.0 1.0
HO A:HAE261 3.0 0.0 1.0
C2 A:HAE261 3.0 0.0 1.0
N A:HAE261 3.1 0.0 1.0
HD2 A:HIS211 3.1 0.0 1.0
OH A:TYR155 3.1 0.0 1.0
CE1 A:HIS211 3.3 0.0 1.0
CE1 A:HIS201 3.5 0.0 1.0
CD2 A:HIS205 3.5 0.0 1.0
HE1 A:HIS211 3.7 0.0 1.0
HE2 A:TYR155 3.8 0.0 1.0
HE1 A:HIS201 3.9 0.0 1.0
HN A:HAE261 4.0 0.0 1.0
CG A:HIS211 4.0 0.0 1.0
HD2 A:HIS205 4.1 0.0 1.0
ND1 A:HIS205 4.1 0.0 1.0
CZ A:TYR155 4.2 0.0 1.0
CG A:HIS201 4.2 0.0 1.0
H31 A:MOP257 4.2 0.0 1.0
ND1 A:HIS211 4.3 0.0 1.0
CG A:HIS205 4.4 0.0 1.0
CE2 A:TYR155 4.4 0.0 1.0
C1 A:HAE261 4.5 0.0 1.0
ND1 A:HIS201 4.5 0.0 1.0
H A:HIS211 4.7 0.0 1.0
HA A:HIS211 4.7 0.0 1.0
H12 A:HAE261 4.7 0.0 1.0
HE3 A:MET219 4.8 0.0 1.0
HE1 A:MET219 4.8 0.0 1.0

Zinc binding site 2 out of 2 in 1ums

Go back to Zinc Binding Sites List in 1ums
Zinc binding site 2 out of 2 in the Stromelysin-1 Catalytic Domain with Hydrophobic Inhibitor Bound, pH 7.0, 32OC, 20 Mm CACL2, 15% Acetonitrile; uc(Nmr) Ensemble of 20 Structures


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Stromelysin-1 Catalytic Domain with Hydrophobic Inhibitor Bound, pH 7.0, 32OC, 20 Mm CACL2, 15% Acetonitrile; uc(Nmr) Ensemble of 20 Structures within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2

b:0.0
occ:1.00
 OD2 A:ASP153 2.3 0.0 1.0
ND1 A:HIS179 2.3 0.0 1.0
NE2 A:HIS151 2.3 0.0 1.0
NE2 A:HIS166 2.3 0.0 1.0
HB2 A:ASP153 2.4 0.0 1.0
CD2 A:HIS151 2.7 0.0 1.0
CG A:HIS179 2.7 0.0 1.0
CE1 A:HIS151 2.8 0.0 1.0
CE1 A:HIS179 2.9 0.0 1.0
CE1 A:HIS166 2.9 0.0 1.0
HB2 A:HIS179 3.0 0.0 1.0
HD2 A:HIS151 3.1 0.0 1.0
CG A:ASP153 3.1 0.0 1.0
CG A:HIS151 3.2 0.0 1.0
HE1 A:HIS166 3.2 0.0 1.0
CB A:ASP153 3.2 0.0 1.0
CD2 A:HIS179 3.2 0.0 1.0
CB A:HIS179 3.2 0.0 1.0
CD2 A:HIS166 3.3 0.0 1.0
HE1 A:HIS151 3.4 0.0 1.0
ND1 A:HIS151 3.4 0.0 1.0
HB3 A:HIS179 3.4 0.0 1.0
NE2 A:HIS179 3.4 0.0 1.0
HB3 A:ASP153 3.4 0.0 1.0
HE1 A:HIS179 3.4 0.0 1.0
HB3 A:HIS151 3.8 0.0 1.0
ND1 A:HIS166 3.8 0.0 1.0
CG A:HIS166 3.9 0.0 1.0
HB A:VAL148 3.9 0.0 1.0
HD2 A:HIS179 3.9 0.0 1.0
HD2 A:HIS166 4.0 0.0 1.0
CB A:HIS151 4.1 0.0 1.0
HE2 A:HIS179 4.2 0.0 1.0
O A:HIS166 4.2 0.0 1.0
HE1 A:TYR168 4.3 0.0 1.0
HB1 A:ALA147 4.3 0.0 1.0
OD1 A:ASP153 4.4 0.0 1.0
HH A:TYR168 4.4 0.0 1.0
CA A:ASP153 4.5 0.0 1.0
H A:ASP153 4.5 0.0 1.0
HB2 A:HIS151 4.6 0.0 1.0
N A:ASP153 4.7 0.0 1.0
CA A:HIS179 4.7 0.0 1.0
HA A:ASP153 4.8 0.0 1.0
CB A:VAL148 4.9 0.0 1.0
HG22 A:VAL148 4.9 0.0 1.0
H A:HIS179 4.9 0.0 1.0
HG21 A:VAL148 4.9 0.0 1.0
HB2 A:ALA147 5.0 0.0 1.0

Reference:

S.R.Van Doren, A.V.Kurochkin, W.Hu, Q.Z.Ye, L.L.Johnson, D.J.Hupe, E.R.Zuiderweg. Solution Structure of the Catalytic Domain of Human Stromelysin Complexed with A Hydrophobic Inhibitor. Protein Sci. V. 4 2487 1995.
ISSN: ISSN 0961-8368
PubMed: 8580839
Page generated: Wed Oct 16 19:33:36 2024

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