Zinc in PDB 1c8t: Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812

All present enzymatic activity of Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812:
3.4.24.17;

The structure of Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812, PDB code: 1c8t was solved by D.L.Steele, O.El-Kabbani, P.Dunten, R.L.Crowther, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	120.100, 47.000, 54.900, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812 also contains other interesting chemical elements:

Calcium

(Ca)

6 atoms

The binding sites of Zinc atom in the Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812 (pdb code 1c8t). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812, PDB code: 1c8t:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn260 b:24.4 occ:1.00 NE2 A:HIS211 1.9 30.3 1.0 NE2 A:HIS201 2.1 24.5 1.0 NE2 A:HIS205 2.4 14.3 1.0 CD2 A:HIS211 2.4 37.1 1.0 SG A:TR1265 2.5 7.5 1.0 CD2 A:HIS201 3.0 18.9 1.0 CE1 A:HIS201 3.1 23.7 1.0 CD2 A:HIS205 3.1 2.5 1.0 CE1 A:HIS211 3.1 19.6 1.0 CB A:TR1265 3.2 12.9 1.0 CE1 A:HIS205 3.5 12.4 1.0 CG A:HIS211 3.7 25.3 1.0 ND1 A:HIS211 4.0 19.2 1.0 N A:TR1265 4.0 18.3 1.0 CA A:TR1265 4.0 16.5 1.0 ND1 A:HIS201 4.1 28.9 1.0 CG A:HIS201 4.1 21.5 1.0 CE A:MET219 4.3 13.6 1.0 CG A:HIS205 4.3 6.1 1.0 NE2 A:GLN202 4.4 16.6 1.0 ND1 A:HIS205 4.5 7.7 1.0 CM2 A:TR1265 4.5 18.8 1.0 O A:MET219 5.0 10.4 1.0 CB A:HIS211 5.0 16.6 1.0

Zinc binding site 2 out of 4 in the Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn261 b:14.2 occ:1.00 ND1 A:HIS179 2.0 8.4 1.0 OD1 A:ASP153 2.2 2.5 1.0 NE2 A:HIS151 2.2 7.1 1.0 NE2 A:HIS166 2.2 4.9 1.0 OD2 A:ASP153 2.9 4.3 1.0 CE1 A:HIS179 2.9 18.5 1.0 CG A:ASP153 2.9 2.0 1.0 CE1 A:HIS151 3.0 4.4 1.0 CG A:HIS179 3.0 4.0 1.0 CE1 A:HIS166 3.1 9.0 1.0 CD2 A:HIS166 3.2 6.6 1.0 CD2 A:HIS151 3.3 2.2 1.0 CB A:HIS179 3.5 13.8 1.0 NE2 A:HIS179 4.1 17.5 1.0 CD2 A:HIS179 4.1 16.4 1.0 OH A:TYR168 4.1 7.2 1.0 ND1 A:HIS151 4.2 5.6 1.0 ND1 A:HIS166 4.2 5.2 1.0 O A:TYR155 4.2 12.6 1.0 CG A:HIS166 4.3 2.3 1.0 CG A:HIS151 4.3 2.3 1.0 CB A:ASP153 4.4 7.5 1.0 CE1 A:PHE157 4.5 9.1 1.0 CE1 A:TYR168 4.5 2.1 1.0 CZ A:PHE157 4.5 10.7 1.0 CZ A:TYR168 4.9 4.8 1.0 CA A:HIS179 5.0 3.1 1.0

Zinc binding site 3 out of 4 in the Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn260 b:21.3 occ:1.00 SG B:TR1265 1.8 17.7 1.0 NE2 B:HIS205 2.0 3.3 1.0 NE2 B:HIS201 2.1 22.8 1.0 NE2 B:HIS211 2.2 32.5 1.0 CB B:TR1265 2.8 12.0 1.0 CE1 B:HIS201 2.9 29.7 1.0 CD2 B:HIS205 2.9 8.0 1.0 CD2 B:HIS211 3.0 19.7 1.0 CE1 B:HIS205 3.1 18.7 1.0 CD2 B:HIS201 3.2 25.3 1.0 CE1 B:HIS211 3.3 29.2 1.0 N B:TR1265 3.5 17.0 1.0 CA B:TR1265 3.6 16.2 1.0 ND1 B:HIS201 4.0 35.1 1.0 CG B:HIS205 4.1 4.1 1.0 ND1 B:HIS205 4.2 4.0 1.0 CG B:HIS201 4.2 26.2 1.0 NE2 B:GLN202 4.2 17.1 1.0 CG B:HIS211 4.2 20.9 1.0 ND1 B:HIS211 4.3 27.1 1.0 CM2 B:TR1265 4.7 17.3 1.0 CB A:PHE86 4.7 28.8 1.0 CG A:PRO87 4.8 25.6 1.0 CD B:GLN202 4.9 16.6 1.0 OE1 B:GLN202 5.0 17.8 1.0

Zinc binding site 4 out of 4 in the Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Human Stromelysin-1 (E202Q) Catalytic Domain Complexed with Ro-26-2812 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn261 b:10.6 occ:1.00 NE2 B:HIS166 2.1 12.2 1.0 OD1 B:ASP153 2.2 19.6 1.0 ND1 B:HIS179 2.3 8.4 1.0 NE2 B:HIS151 2.4 11.7 1.0 CE1 B:HIS166 2.9 14.9 1.0 CG B:ASP153 3.0 5.8 1.0 CD2 B:HIS151 3.0 3.7 1.0 OD2 B:ASP153 3.1 9.0 1.0 CG B:HIS179 3.2 2.0 1.0 CD2 B:HIS166 3.3 6.5 1.0 CE1 B:HIS179 3.3 8.8 1.0 CE1 B:HIS151 3.5 4.1 1.0 CB B:HIS179 3.5 6.8 1.0 O B:TYR155 4.1 12.1 1.0 ND1 B:HIS166 4.1 15.4 1.0 OH B:TYR168 4.2 13.3 1.0 CG B:HIS151 4.3 3.4 1.0 CG B:HIS166 4.3 7.3 1.0 NE2 B:HIS179 4.4 10.4 1.0 CD2 B:HIS179 4.4 3.1 1.0 CZ B:PHE157 4.4 16.2 1.0 CB B:ASP153 4.4 7.4 1.0 CE1 B:PHE157 4.4 5.8 1.0 ND1 B:HIS151 4.5 4.1 1.0 CE1 B:TYR168 4.6 8.5 1.0 O B:HOH28 4.8 9.3 1.0 CZ B:TYR168 4.9 11.6 1.0 CA B:HIS179 4.9 7.9 1.0

D.L.Steele, O.El-Kabbani, P.Dunten, L.J.Windsor, R.U.Kammlott, R.L.Crowther, C.Michoud, J.A.Engler, J.J.Birktoft. Expression, Characterization and Structure Determination of An Active Site Mutant (GLU202-Gln) of Mini-Stromelysin-1. Protein Eng. V. 13 397 2000.
ISSN: ISSN 0269-2139
PubMed: 10877850
DOI: 10.1093/PROTEIN/13.6.397