Calcium in PDB 1bm6: Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to A Potent Non-Peptidic Inhibitor, uc(Nmr), 20 Structures

All present enzymatic activity of Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to A Potent Non-Peptidic Inhibitor, uc(Nmr), 20 Structures:
3.4.24.17;

The structure of Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to A Potent Non-Peptidic Inhibitor, uc(Nmr), 20 Structures also contains other interesting chemical elements:

Zinc

(Zn)

40 atoms

The binding sites of Calcium atom in the Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to A Potent Non-Peptidic Inhibitor, uc(Nmr), 20 Structures (pdb code 1bm6). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to A Potent Non-Peptidic Inhibitor, uc(Nmr), 20 Structures, PDB code: 1bm6:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to A Potent Non-Peptidic Inhibitor, uc(Nmr), 20 Structures


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to A Potent Non-Peptidic Inhibitor, uc(Nmr), 20 Structures within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca258 b:0.0 occ:1.00 HA2 A:GLY159 2.4 0.0 1.0 O A:ASP158 2.5 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 OD2 A:ASP181 2.6 0.0 1.0 OE2 A:GLU184 2.6 0.0 1.0 OD1 A:ASP158 2.6 0.0 1.0 H A:GLY161 2.8 0.0 1.0 CA A:GLY159 2.8 0.0 1.0 C A:ASP158 2.8 0.0 1.0 C A:GLY159 2.9 0.0 1.0 N A:GLY159 3.0 0.0 1.0 C A:VAL163 3.4 0.0 1.0 HA A:LEU164 3.4 0.0 1.0 N A:GLY161 3.5 0.0 1.0 C A:GLY161 3.5 0.0 1.0 CG A:ASP181 3.6 0.0 1.0 H A:ASP158 3.6 0.0 1.0 HB A:VAL163 3.6 0.0 1.0 H A:GLY159 3.7 0.0 1.0 CG A:ASP158 3.8 0.0 1.0 CD A:GLU184 3.8 0.0 1.0 HA3 A:GLY159 3.9 0.0 1.0 CA A:GLY161 3.9 0.0 1.0 N A:PRO160 3.9 0.0 1.0 HA3 A:GLY161 4.0 0.0 1.0 HD13 A:LEU164 4.0 0.0 1.0 CA A:ASP158 4.0 0.0 1.0 HB2 A:ASP181 4.0 0.0 1.0 N A:VAL163 4.1 0.0 1.0 N A:LEU164 4.1 0.0 1.0 N A:ASP158 4.1 0.0 1.0 CA A:VAL163 4.2 0.0 1.0 CA A:LEU164 4.2 0.0 1.0 H A:VAL163 4.2 0.0 1.0 CB A:ASP181 4.3 0.0 1.0 OD1 A:ASP181 4.4 0.0 1.0 HG2 A:GLU184 4.4 0.0 1.0 HD2 A:PHE157 4.4 0.0 1.0 C A:ASN162 4.4 0.0 1.0 CB A:VAL163 4.4 0.0 1.0 C A:PRO160 4.4 0.0 1.0 CB A:ASP158 4.4 0.0 1.0 HB3 A:ASP181 4.6 0.0 1.0 N A:ASN162 4.6 0.0 1.0 HD2 A:PRO160 4.6 0.0 1.0 HB2 A:ASP158 4.6 0.0 1.0 OE1 A:GLU184 4.7 0.0 1.0 O A:ASN162 4.7 0.0 1.0 CA A:PRO160 4.7 0.0 1.0 CG A:GLU184 4.7 0.0 1.0 OD2 A:ASP158 4.8 0.0 1.0 H A:LEU164 4.9 0.0 1.0 CD A:PRO160 4.9 0.0 1.0 HA A:ASP158 4.9 0.0 1.0 HA2 A:GLY161 4.9 0.0 1.0 HG A:LEU164 5.0 0.0 1.0 C A:LEU164 5.0 0.0 1.0 HG22 A:VAL163 5.0 0.0 1.0 CD1 A:LEU164 5.0 0.0 1.0

Calcium binding site 2 out of 2 in the Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to A Potent Non-Peptidic Inhibitor, uc(Nmr), 20 Structures


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to A Potent Non-Peptidic Inhibitor, uc(Nmr), 20 Structures within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca259 b:0.0 occ:1.00 O A:GLY176 2.4 0.0 1.0 OD1 A:ASP177 2.5 0.0 1.0 O A:ASN175 2.6 0.0 1.0 O A:GLY173 2.7 0.0 1.0 O A:ASP141 2.7 0.0 1.0 C A:ASN175 2.7 0.0 1.0 N A:GLY176 3.1 0.0 1.0 C A:GLY176 3.2 0.0 1.0 N A:ASN175 3.2 0.0 1.0 HB3 A:ASN175 3.2 0.0 1.0 H A:ASN175 3.3 0.0 1.0 CA A:ASN175 3.4 0.0 1.0 CG A:ASP177 3.5 0.0 1.0 CA A:GLY176 3.5 0.0 1.0 HA3 A:GLY176 3.5 0.0 1.0 HA A:ASP141 3.5 0.0 1.0 C A:ASP141 3.5 0.0 1.0 C A:ILE174 3.6 0.0 1.0 H A:GLY176 3.7 0.0 1.0 C A:GLY173 3.7 0.0 1.0 CB A:ASN175 3.8 0.0 1.0 O A:ALA140 3.8 0.0 1.0 OD2 A:ASP177 3.9 0.0 1.0 H A:MET143 3.9 0.0 1.0 HA A:ILE174 4.0 0.0 1.0 CA A:ASP141 4.1 0.0 1.0 O A:ILE174 4.1 0.0 1.0 HA A:ILE142 4.2 0.0 1.0 HB2 A:ASN175 4.2 0.0 1.0 CA A:ILE174 4.2 0.0 1.0 N A:ASP177 4.3 0.0 1.0 HA A:ASN175 4.4 0.0 1.0 N A:ILE174 4.4 0.0 1.0 HA2 A:GLY173 4.4 0.0 1.0 N A:ILE142 4.5 0.0 1.0 HA2 A:GLY176 4.5 0.0 1.0 CB A:ASP177 4.6 0.0 1.0 C A:ALA140 4.7 0.0 1.0 HA A:ASP177 4.7 0.0 1.0 CA A:GLY173 4.7 0.0 1.0 HB2 A:MET143 4.7 0.0 1.0 CA A:ASP177 4.8 0.0 1.0 N A:MET143 4.8 0.0 1.0 CA A:ILE142 4.8 0.0 1.0 HB2 A:ASP177 4.9 0.0 1.0 N A:ASP141 4.9 0.0 1.0 HD21 A:ASN175 4.9 0.0 1.0 HB2 A:GLU139 4.9 0.0 1.0

Y.C.Li, X.Zhang, R.Melton, V.Ganu, N.C.Gonnella. Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to A Potent, Nonpeptidic Inhibitor. Biochemistry V. 37 14048 1998.
ISSN: ISSN 0006-2960
PubMed: 9760240
DOI: 10.1021/BI981328W