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Calcium in PDB 1slm: Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme

Enzymatic activity of Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme

All present enzymatic activity of Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme:
3.4.24.17;

Protein crystallography data

The structure of Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme, PDB code: 1slm was solved by J.W.Becker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group F 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 111.040, 145.560, 76.750, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 25.6

Other elements in 1slm:

The structure of Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme (pdb code 1slm). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme, PDB code: 1slm:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1slm

Go back to Calcium Binding Sites List in 1slm
Calcium binding site 1 out of 2 in the Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca259

b:19.1
occ:1.00
O A:GLY159 2.3 22.6 1.0
O A:VAL163 2.3 20.1 1.0
OE2 A:GLU184 2.4 21.2 1.0
OD2 A:ASP181 2.4 17.8 1.0
O A:GLY161 2.4 19.8 1.0
OD1 A:ASP158 2.5 24.2 1.0
C A:VAL163 3.5 18.6 1.0
CG A:ASP181 3.5 15.5 1.0
C A:GLY159 3.5 18.3 1.0
H A:ASP158 3.6 0.0 1.0
CD A:GLU184 3.6 18.1 1.0
C A:GLY161 3.6 18.4 1.0
CG A:ASP158 3.7 21.9 1.0
N A:GLY161 4.0 19.4 1.0
N A:VAL163 4.0 16.9 1.0
H A:VAL163 4.0 0.0 1.0
C A:PRO160 4.1 22.2 1.0
H A:GLY161 4.1 0.0 1.0
CB A:ASP181 4.1 13.8 1.0
CA A:VAL163 4.2 17.0 1.0
N A:GLY159 4.2 19.9 1.0
C A:ASP158 4.2 19.3 1.0
CA A:PRO160 4.3 19.5 1.0
OD2 A:ASP158 4.3 24.5 1.0
N A:ASP158 4.3 21.5 1.0
C A:ASN162 4.4 16.8 1.0
N A:PRO160 4.4 18.2 1.0
OD1 A:ASP181 4.4 17.1 1.0
OE1 A:GLU184 4.4 23.2 1.0
CA A:GLY161 4.4 20.1 1.0
O A:ASP158 4.4 20.4 1.0
H A:GLY159 4.5 0.0 1.0
N A:LEU164 4.5 20.0 1.0
CA A:GLY159 4.5 18.4 1.0
O A:PRO160 4.5 25.2 1.0
CG A:GLU184 4.5 21.2 1.0
CB A:VAL163 4.6 16.3 1.0
CA A:ASP158 4.6 22.2 1.0
N A:ASN162 4.6 20.6 1.0
CA A:LEU164 4.7 18.6 1.0
CB A:ASP158 4.7 21.9 1.0
O A:ASN162 4.8 17.9 1.0
CA A:ASN162 4.9 18.9 1.0
O A:HOH503 4.9 35.4 1.0
CB A:ASN162 5.0 21.1 1.0

Calcium binding site 2 out of 2 in 1slm

Go back to Calcium Binding Sites List in 1slm
Calcium binding site 2 out of 2 in the Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca260

b:38.7
occ:1.00
O A:GLY173 2.3 19.6 1.0
O A:ASN175 2.4 20.6 1.0
O A:HOH306 2.4 16.2 1.0
O A:ASP141 2.5 20.9 1.0
O A:HOH312 2.5 40.5 1.0
OD1 A:ASP177 2.9 18.2 1.0
H2 A:HOH306 3.1 0.0 1.0
H1 A:HOH306 3.2 0.0 1.0
H2 A:HOH312 3.2 0.0 1.0
H1 A:HOH312 3.2 0.0 1.0
C A:GLY173 3.5 21.0 1.0
C A:ASN175 3.6 18.9 1.0
C A:ASP141 3.6 19.1 1.0
CG A:ASP177 3.8 16.2 1.0
C A:ILE174 4.0 20.3 1.0
H A:ASP177 4.0 0.0 1.0
N A:ASN175 4.1 20.9 1.0
O A:ALA140 4.1 23.1 1.0
O A:ILE174 4.2 21.7 1.0
O A:GLY171 4.2 21.4 1.0
H A:MET143 4.2 0.0 1.0
OD2 A:ASP177 4.2 16.9 1.0
N A:ASP177 4.3 15.2 1.0
CA A:ASP141 4.3 20.1 1.0
N A:GLY173 4.4 24.2 1.0
N A:ILE174 4.4 21.4 1.0
CA A:GLY173 4.4 22.0 1.0
CA A:ILE174 4.4 20.3 1.0
N A:GLY176 4.4 18.6 1.0
H A:ASN175 4.4 0.0 1.0
CA A:GLY176 4.4 14.7 1.0
CA A:ASN175 4.5 17.1 1.0
O A:HOH328 4.5 26.2 1.0
N A:ILE142 4.6 19.4 1.0
H A:GLY173 4.6 0.0 1.0
C A:GLY176 4.6 12.1 1.0
C A:PRO172 4.6 21.8 1.0
CA A:ILE142 4.7 16.6 1.0
O A:HOH324 4.8 32.1 1.0
O A:PRO172 4.8 21.7 1.0
N A:MET143 4.9 17.7 1.0
CB A:ASP177 4.9 15.1 1.0
CG A:MET143 4.9 21.2 1.0
CH2 A:TRP92 5.0 15.1 1.0

Reference:

J.W.Becker, A.I.Marcy, L.L.Rokosz, M.G.Axel, J.J.Burbaum, P.M.Fitzgerald, P.M.Cameron, C.K.Esser, W.K.Hagmann, J.D.Hermes, J.P.Springer. Stromelysin-1: Three-Dimensional Structure of the Inhibited Catalytic Domain and of the C-Truncated Proenzyme. Protein Sci. V. 4 1966 1995.
ISSN: ISSN 0961-8368
PubMed: 8535233
Page generated: Sat Dec 12 03:19:32 2020

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