Zinc 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:

Calcium

(Ca)

40 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc 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 Zinc binding site number: 1; 2;

Zinc 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 Zinc with other atoms in the Zn 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:Zn256 b:0.0 occ:1.00 NE2 A:HIS205 2.2 0.0 1.0 NE2 A:HIS211 2.2 0.0 1.0 NE2 A:HIS201 2.2 0.0 1.0 O1 A:HAV1 2.3 0.0 1.0 O A:HAV1 2.7 0.0 1.0 HG2 A:MET219 3.0 0.0 1.0 HO1 A:HAV1 3.0 0.0 1.0 CE1 A:HIS211 3.0 0.0 1.0 CD2 A:HIS205 3.0 0.0 1.0 CE1 A:HIS201 3.1 0.0 1.0 CD2 A:HIS201 3.2 0.0 1.0 CE1 A:HIS205 3.2 0.0 1.0 CD2 A:HIS211 3.2 0.0 1.0 N A:HAV1 3.2 0.0 1.0 HE1 A:HIS211 3.2 0.0 1.0 HD2 A:HIS205 3.2 0.0 1.0 HE1 A:HIS201 3.3 0.0 1.0 C A:HAV1 3.3 0.0 1.0 HD2 A:HIS201 3.4 0.0 1.0 HE1 A:HIS205 3.5 0.0 1.0 HD2 A:HIS211 3.5 0.0 1.0 HG3 A:MET219 3.5 0.0 1.0 CG A:MET219 3.7 0.0 1.0 HG11 A:HAV1 4.0 0.0 1.0 HN A:HAV1 4.1 0.0 1.0 ND1 A:HIS211 4.2 0.0 1.0 ND1 A:HIS201 4.2 0.0 1.0 CG A:HIS205 4.2 0.0 1.0 HB1 A:3MP2 4.2 0.0 1.0 ND1 A:HIS205 4.2 0.0 1.0 CG A:HIS201 4.2 0.0 1.0 CG A:HIS211 4.3 0.0 1.0 O A:PHE210 4.4 0.0 1.0 SD A:MET219 4.4 0.0 1.0 HE1 A:MET219 4.5 0.0 1.0 CA A:HAV1 4.8 0.0 1.0 HE3 A:MET219 4.9 0.0 1.0 CE A:MET219 4.9 0.0 1.0 HA A:MET219 5.0 0.0 1.0 CG1 A:HAV1 5.0 0.0 1.0 HD1 A:HIS211 5.0 0.0 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn257 b:0.0 occ:1.00 HE1 A:PHE157 1.7 0.0 1.0 ND1 A:HIS179 2.2 0.0 1.0 NE2 A:HIS151 2.2 0.0 1.0 NE2 A:HIS166 2.3 0.0 1.0 CE1 A:PHE157 2.4 0.0 1.0 HD1 A:PHE157 2.5 0.0 1.0 CD1 A:PHE157 2.8 0.0 1.0 CE1 A:HIS179 2.9 0.0 1.0 CD2 A:HIS151 3.0 0.0 1.0 HE1 A:HIS179 3.0 0.0 1.0 CE1 A:HIS166 3.1 0.0 1.0 HD2 A:HIS151 3.2 0.0 1.0 CE1 A:HIS151 3.2 0.0 1.0 CD2 A:HIS166 3.2 0.0 1.0 HB3 A:HIS179 3.3 0.0 1.0 HE1 A:HIS166 3.3 0.0 1.0 CG A:HIS179 3.3 0.0 1.0 HE1 A:HIS151 3.5 0.0 1.0 HB2 A:TYR155 3.6 0.0 1.0 HD2 A:HIS166 3.6 0.0 1.0 CZ A:PHE157 3.6 0.0 1.0 HD1 A:TYR155 3.7 0.0 1.0 CB A:HIS179 3.8 0.0 1.0 O A:TYR155 3.8 0.0 1.0 HZ A:PHE157 4.0 0.0 1.0 CG A:PHE157 4.1 0.0 1.0 ND1 A:HIS166 4.1 0.0 1.0 NE2 A:HIS179 4.1 0.0 1.0 CG A:HIS151 4.2 0.0 1.0 ND1 A:HIS151 4.2 0.0 1.0 CG A:HIS166 4.2 0.0 1.0 CD2 A:HIS179 4.3 0.0 1.0 HB2 A:HIS179 4.4 0.0 1.0 HB2 A:ALA147 4.4 0.0 1.0 CD1 A:TYR155 4.4 0.0 1.0 HB1 A:ALA147 4.5 0.0 1.0 CB A:TYR155 4.6 0.0 1.0 HE1 A:TYR168 4.7 0.0 1.0 CE2 A:PHE157 4.7 0.0 1.0 OH A:TYR168 4.8 0.0 1.0 HB2 A:PHE157 4.8 0.0 1.0 C A:TYR155 4.9 0.0 1.0 CD2 A:PHE157 4.9 0.0 1.0 HE2 A:HIS179 4.9 0.0 1.0 CG A:TYR155 4.9 0.0 1.0 HD1 A:HIS166 4.9 0.0 1.0 O A:HIS166 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