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Calcium 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:

Zinc (Zn) 40 atoms

Calcium Binding Sites:

The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was 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:

Calcium binding site 1 out of 1 in 1ums

Go back to Calcium Binding Sites List in 1ums
Calcium binding site 1 out of 1 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 Calcium with other atoms in the Ca 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:Ca3

b:0.0
occ:1.00
OE2 A:GLU184 2.3 0.0 1.0
OD1 A:ASP158 2.3 0.0 1.0
OD2 A:ASP181 2.3 0.0 1.0
O A:GLY159 2.6 0.0 1.0
O A:VAL163 2.6 0.0 1.0
O A:GLY161 2.6 0.0 1.0
HB2 A:ASN162 2.7 0.0 1.0
CD A:GLU184 3.0 0.0 1.0
HB2 A:ASP158 3.1 0.0 1.0
CG A:ASP158 3.1 0.0 1.0
C A:GLY161 3.2 0.0 1.0
OE1 A:GLU184 3.2 0.0 1.0
HG23 A:THR193 3.3 0.0 1.0
C A:ASP158 3.3 0.0 1.0
CB A:ASP158 3.3 0.0 1.0
N A:GLY159 3.4 0.0 1.0
H A:ASP158 3.4 0.0 1.0
H A:GLY159 3.4 0.0 1.0
H A:GLY161 3.5 0.0 1.0
CG A:ASP181 3.5 0.0 1.0
CA A:ASP158 3.6 0.0 1.0
C A:GLY159 3.7 0.0 1.0
N A:ASN162 3.7 0.0 1.0
CB A:ASN162 3.7 0.0 1.0
N A:ASP158 3.7 0.0 1.0
C A:VAL163 3.8 0.0 1.0
O A:ASP158 3.8 0.0 1.0
HD11 A:LEU164 3.8 0.0 1.0
CA A:ASN162 3.9 0.0 1.0
HB3 A:LEU164 3.9 0.0 1.0
C A:ASN162 3.9 0.0 1.0
N A:GLY161 4.0 0.0 1.0
HA A:LEU164 4.1 0.0 1.0
CA A:GLY159 4.1 0.0 1.0
N A:VAL163 4.2 0.0 1.0
OD2 A:ASP158 4.2 0.0 1.0
CG2 A:THR193 4.2 0.0 1.0
CA A:GLY161 4.2 0.0 1.0
HB2 A:ASP181 4.3 0.0 1.0
HA A:PRO160 4.3 0.0 1.0
CG A:GLU184 4.3 0.0 1.0
HG21 A:THR193 4.3 0.0 1.0
HB3 A:ASN162 4.3 0.0 1.0
H A:VAL163 4.3 0.0 1.0
O A:ASN162 4.3 0.0 1.0
OD1 A:ASP181 4.4 0.0 1.0
H A:ASN162 4.4 0.0 1.0
HB3 A:ASP158 4.4 0.0 1.0
HG2 A:GLU184 4.4 0.0 1.0
CB A:ASP181 4.5 0.0 1.0
HG3 A:GLU184 4.5 0.0 1.0
HB3 A:ASP181 4.6 0.0 1.0
HA A:ASP158 4.6 0.0 1.0
HH2 A:TRP186 4.7 0.0 1.0
CG A:ASN162 4.7 0.0 1.0
HB3 A:ASP183 4.7 0.0 1.0
HD21 A:ASN162 4.7 0.0 1.0
HA2 A:GLY159 4.7 0.0 1.0
CA A:VAL163 4.7 0.0 1.0
CA A:LEU164 4.7 0.0 1.0
N A:LEU164 4.8 0.0 1.0
N A:PRO160 4.8 0.0 1.0
CB A:LEU164 4.8 0.0 1.0
C A:PHE157 4.8 0.0 1.0
C A:PRO160 4.8 0.0 1.0
HG22 A:THR193 4.8 0.0 1.0
CA A:PRO160 4.9 0.0 1.0
CD1 A:LEU164 4.9 0.0 1.0
HA2 A:GLY161 4.9 0.0 1.0
HB A:THR193 5.0 0.0 1.0
HA3 A:GLY159 5.0 0.0 1.0
HA3 A:GLY161 5.0 0.0 1.0
HA A:ASN162 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: Sat Dec 12 03:23:12 2020

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