Zinc in PDB 1c3i: Human Stromelysin-1 Catalytic Domain Complexed with Ro-26-2812

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

The structure of Human Stromelysin-1 Catalytic Domain Complexed with Ro-26-2812, PDB code: 1c3i was solved by D.L.Steele, R.U.Kammlott, R.L.Crowther, J.J.Birktoft, P.Dunten, J.E.Engler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.83
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	37.730, 78.060, 105.740, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Human Stromelysin-1 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 Catalytic Domain Complexed with Ro-26-2812 (pdb code 1c3i). 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 Catalytic Domain Complexed with Ro-26-2812, PDB code: 1c3i:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Human Stromelysin-1 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 Catalytic Domain Complexed with Ro-26-2812 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn260 b:8.5 occ:1.00 NE2 A:HIS201 1.9 3.0 1.0 NE2 A:HIS211 1.9 11.2 1.0 NE2 A:HIS205 2.1 8.1 1.0 CD2 A:HIS211 2.8 8.7 1.0 CD2 A:HIS201 2.9 2.0 1.0 CE1 A:HIS201 2.9 2.0 1.0 CE1 A:HIS205 3.0 5.6 1.0 CE1 A:HIS211 3.0 10.7 1.0 CD2 A:HIS205 3.2 2.0 1.0 O A:HOH383 3.6 19.1 1.0 CG A:HIS211 4.0 10.9 1.0 CG A:HIS201 4.0 2.0 1.0 ND1 A:HIS201 4.1 2.8 1.0 ND1 A:HIS211 4.1 7.6 1.0 ND1 A:HIS205 4.1 6.5 1.0 CG A:HIS205 4.3 2.0 1.0 O A:HOH292 4.3 12.0 1.0 CE A:MET219 4.8 2.0 1.0 OE1 A:GLU202 4.9 7.9 1.0 CE1 A:TYR223 5.0 2.0 1.0

Zinc binding site 2 out of 4 in the Human Stromelysin-1 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 Catalytic Domain Complexed with Ro-26-2812 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn261 b:9.5 occ:1.00 OD2 A:ASP153 1.9 6.4 1.0 NE2 A:HIS166 2.0 2.0 1.0 NE2 A:HIS151 2.0 2.0 1.0 ND1 A:HIS179 2.0 8.8 1.0 CG A:ASP153 2.8 2.2 1.0 CE1 A:HIS179 2.9 2.0 1.0 CE1 A:HIS166 2.9 8.0 1.0 CE1 A:HIS151 3.0 2.0 1.0 CD2 A:HIS151 3.0 2.0 1.0 CD2 A:HIS166 3.0 2.0 1.0 OD1 A:ASP153 3.1 2.0 1.0 CG A:HIS179 3.1 2.8 1.0 CB A:HIS179 3.5 2.0 1.0 NE2 A:HIS179 4.0 2.5 1.0 ND1 A:HIS151 4.1 5.6 1.0 ND1 A:HIS166 4.1 2.0 1.0 OH A:TYR168 4.1 2.0 1.0 CG A:HIS151 4.1 6.5 1.0 CG A:HIS166 4.1 3.9 1.0 CB A:ASP153 4.2 5.9 1.0 CD2 A:HIS179 4.2 2.0 1.0 O A:TYR155 4.3 8.9 1.0 CE1 A:TYR168 4.6 5.0 1.0 CZ A:PHE157 4.8 5.1 1.0 CE1 A:PHE157 4.8 8.0 1.0 CZ A:TYR168 4.9 2.0 1.0 CA A:HIS179 5.0 2.6 1.0

Zinc binding site 3 out of 4 in the Human Stromelysin-1 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 Catalytic Domain Complexed with Ro-26-2812 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn260 b:11.4 occ:1.00 NE2 B:HIS211 1.8 2.0 1.0 NE2 B:HIS201 2.1 6.3 1.0 SG B:TR11 2.1 7.2 1.0 NE2 B:HIS205 2.2 9.8 1.0 CE1 B:HIS211 2.8 6.3 1.0 CD2 B:HIS211 2.9 11.1 1.0 CE1 B:HIS201 3.1 6.5 1.0 CD2 B:HIS205 3.1 9.8 1.0 CD2 B:HIS201 3.1 6.6 1.0 CE1 B:HIS205 3.2 7.7 1.0 CB B:TR11 3.3 7.9 1.0 N B:TR11 3.6 8.8 1.0 ND1 B:HIS211 3.9 2.0 1.0 CG B:HIS211 4.0 3.6 1.0 CA B:TR11 4.1 9.1 1.0 ND1 B:HIS201 4.2 2.0 1.0 CG B:HIS201 4.3 5.0 1.0 CG B:HIS205 4.3 9.6 1.0 ND1 B:HIS205 4.3 9.0 1.0 O B:HOH353 4.3 8.1 1.0 OE1 B:GLU202 4.3 6.7 1.0 CM2 B:TR11 4.5 7.5 1.0 OE2 B:GLU202 4.5 5.1 1.0 CD B:GLU202 4.8 11.6 1.0 CE B:MET219 4.9 8.3 1.0

Zinc binding site 4 out of 4 in the Human Stromelysin-1 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 Catalytic Domain Complexed with Ro-26-2812 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn261 b:10.7 occ:1.00 NE2 B:HIS151 1.9 7.9 1.0 OD2 B:ASP153 1.9 8.7 1.0 NE2 B:HIS166 2.1 8.5 1.0 ND1 B:HIS179 2.1 8.5 1.0 CE1 B:HIS151 2.7 8.0 1.0 CG B:ASP153 2.8 13.8 1.0 CE1 B:HIS166 2.9 10.1 1.0 CE1 B:HIS179 2.9 4.3 1.0 OD1 B:ASP153 3.0 12.8 1.0 CD2 B:HIS151 3.1 5.9 1.0 CG B:HIS179 3.1 13.2 1.0 CD2 B:HIS166 3.2 9.0 1.0 CB B:HIS179 3.6 5.8 1.0 OH B:TYR168 3.9 8.9 1.0 ND1 B:HIS151 3.9 2.0 1.0 NE2 B:HIS179 4.1 7.8 1.0 ND1 B:HIS166 4.1 9.8 1.0 CG B:HIS151 4.1 6.5 1.0 CB B:ASP153 4.1 8.9 1.0 O B:TYR155 4.1 9.0 1.0 CD2 B:HIS179 4.2 2.0 1.0 CG B:HIS166 4.3 7.6 1.0 CE1 B:PHE157 4.5 2.6 1.0 CE1 B:TYR168 4.5 7.5 1.0 CZ B:PHE157 4.7 5.2 1.0 CZ B:TYR168 4.7 8.4 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