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Calcium in PDB 1umt: Stromelysin-1 Catalytic Domain with Hydrophobic Inhibitor Bound, pH 7.0, 32OC, 20 Mm CACL2, 15% Acetonitrile; uc(Nmr) Average of 20 Structures Minimized with Restraints

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

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

Other elements in 1umt:

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

Zinc (Zn) 2 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) Average of 20 Structures Minimized with Restraints (pdb code 1umt). 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) Average of 20 Structures Minimized with Restraints, PDB code: 1umt:

Calcium binding site 1 out of 1 in 1umt

Go back to Calcium Binding Sites List in 1umt
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) Average of 20 Structures Minimized with Restraints


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) Average of 20 Structures Minimized with Restraints within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca3

b:0.0
occ:1.00
OD1 A:ASP158 2.3 0.0 1.0
OE2 A:GLU184 2.3 0.0 1.0
HB2 A:ASN162 2.3 0.0 1.0
OD2 A:ASP181 2.3 0.0 1.0
HD11 A:LEU164 2.4 0.0 1.0
O A:GLY159 2.6 0.0 1.0
O A:GLY161 2.6 0.0 1.0
O A:VAL163 2.6 0.0 1.0
CG A:ASP158 3.0 0.0 1.0
HD13 A:LEU164 3.1 0.0 1.0
HB3 A:LEU164 3.1 0.0 1.0
CD1 A:LEU164 3.2 0.0 1.0
C A:GLY161 3.2 0.0 1.0
CB A:ASN162 3.3 0.0 1.0
CD A:GLU184 3.4 0.0 1.0
H A:VAL163 3.4 0.0 1.0
HG23 A:THR193 3.5 0.0 1.0
OD2 A:ASP158 3.5 0.0 1.0
CG A:ASP181 3.5 0.0 1.0
N A:ASN162 3.6 0.0 1.0
CA A:ASN162 3.6 0.0 1.0
N A:VAL163 3.6 0.0 1.0
C A:VAL163 3.6 0.0 1.0
C A:ASN162 3.7 0.0 1.0
C A:GLY159 3.7 0.0 1.0
HB3 A:ASN162 3.8 0.0 1.0
C A:ASP158 3.8 0.0 1.0
OE1 A:GLU184 3.9 0.0 1.0
N A:GLY159 3.9 0.0 1.0
HD12 A:LEU164 3.9 0.0 1.0
CB A:ASP158 4.0 0.0 1.0
CB A:LEU164 4.0 0.0 1.0
O A:ASP158 4.0 0.0 1.0
HB2 A:ASP158 4.1 0.0 1.0
HD21 A:ASN162 4.1 0.0 1.0
CG A:LEU164 4.1 0.0 1.0
H A:GLY159 4.2 0.0 1.0
N A:GLY161 4.2 0.0 1.0
OD1 A:ASP181 4.3 0.0 1.0
CA A:VAL163 4.3 0.0 1.0
H A:ASP158 4.3 0.0 1.0
HB2 A:ASP181 4.3 0.0 1.0
CG A:ASN162 4.3 0.0 1.0
H A:GLY161 4.3 0.0 1.0
CA A:ASP158 4.3 0.0 1.0
HA A:VAL163 4.3 0.0 1.0
O A:ASN162 4.3 0.0 1.0
H A:ASN162 4.4 0.0 1.0
CA A:GLY159 4.4 0.0 1.0
CA A:GLY161 4.4 0.0 1.0
CG2 A:THR193 4.4 0.0 1.0
HG21 A:THR193 4.5 0.0 1.0
HA A:PRO160 4.5 0.0 1.0
HG2 A:GLU184 4.5 0.0 1.0
C A:PRO160 4.5 0.0 1.0
CB A:ASP181 4.6 0.0 1.0
ND2 A:ASN162 4.6 0.0 1.0
CG A:GLU184 4.6 0.0 1.0
N A:ASP158 4.6 0.0 1.0
N A:LEU164 4.6 0.0 1.0
HG A:LEU164 4.7 0.0 1.0
HB2 A:LEU164 4.7 0.0 1.0
HA A:ASN162 4.7 0.0 1.0
N A:PRO160 4.7 0.0 1.0
HA A:LEU164 4.8 0.0 1.0
HA2 A:GLY159 4.8 0.0 1.0
CA A:PRO160 4.8 0.0 1.0
CA A:LEU164 4.8 0.0 1.0
HB3 A:ASP181 4.8 0.0 1.0
HG22 A:THR193 4.9 0.0 1.0
HG3 A:GLU184 4.9 0.0 1.0
HB3 A:ASP158 4.9 0.0 1.0
O A:PRO160 4.9 0.0 1.0
HA2 A:GLY161 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 03:23:10 2020

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