Zinc in PDB 1slm: 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;

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

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

Calcium

(Ca)

2 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Fibroblast Stromelysin-1: the C-Truncated Human Proenzyme, PDB code: 1slm:
Jump to Zinc binding site number: 1; 2;

Zinc 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 Zinc with other atoms in the Zn 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:Zn257 b:20.0 occ:1.00 NE2 A:HIS201 1.8 11.7 1.0 NE2 A:HIS211 1.9 21.7 1.0 NE2 A:HIS205 1.9 18.3 1.0 SG A:CYS75 2.2 16.2 1.0 CD2 A:HIS201 2.8 11.6 1.0 CD2 A:HIS211 2.9 17.2 1.0 CE1 A:HIS211 2.9 15.4 1.0 CE1 A:HIS201 2.9 13.1 1.0 CE1 A:HIS205 2.9 17.1 1.0 CB A:CYS75 3.0 15.2 1.0 CD2 A:HIS205 3.0 14.2 1.0 ND1 A:HIS211 4.0 14.7 1.0 ND1 A:HIS201 4.0 11.3 1.0 CG A:HIS201 4.0 11.1 1.0 CG A:HIS211 4.0 16.2 1.0 ND1 A:HIS205 4.1 14.5 1.0 CB A:VAL77 4.1 17.6 1.0 CG A:HIS205 4.1 16.1 1.0 H A:VAL77 4.2 0.0 1.0 OE2 A:GLU202 4.2 14.1 1.0 CG2 A:VAL77 4.4 16.3 1.0 OE1 A:GLU202 4.4 17.3 1.0 CA A:CYS75 4.4 14.9 1.0 CD A:GLU202 4.6 14.0 1.0 CE A:MET219 4.8 12.9 1.0 HD1 A:HIS211 4.8 0.0 1.0 HD1 A:HIS201 4.9 0.0 1.0 N A:VAL77 4.9 17.9 1.0 CG1 A:VAL77 4.9 18.3 1.0 C A:CYS75 4.9 15.7 1.0 HD1 A:HIS205 5.0 0.0 1.0 O A:VAL77 5.0 20.9 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn258 b:21.2 occ:1.00 NE2 A:HIS151 1.8 19.3 1.0 NE2 A:HIS166 1.8 14.6 1.0 OD2 A:ASP153 1.9 16.7 1.0 ND1 A:HIS179 1.9 18.4 1.0 CE1 A:HIS166 2.6 14.8 1.0 CD2 A:HIS151 2.7 20.6 1.0 CE1 A:HIS179 2.8 16.8 1.0 CE1 A:HIS151 2.9 18.4 1.0 CG A:ASP153 2.9 17.8 1.0 CG A:HIS179 3.0 14.3 1.0 CD2 A:HIS166 3.1 14.6 1.0 OD1 A:ASP153 3.3 20.6 1.0 CB A:HIS179 3.5 13.9 1.0 OH A:TYR168 3.7 26.5 1.0 ND1 A:HIS166 3.8 12.3 1.0 CG A:HIS151 3.9 19.2 1.0 ND1 A:HIS151 4.0 16.4 1.0 NE2 A:HIS179 4.0 17.1 1.0 CG A:HIS166 4.1 13.4 1.0 CD2 A:HIS179 4.1 14.4 1.0 CB A:ASP153 4.3 22.3 1.0 O A:TYR155 4.3 27.3 1.0 HH A:TYR168 4.4 0.0 1.0 CE2 A:TYR168 4.5 21.6 1.0 CZ A:TYR168 4.5 24.2 1.0 CZ A:PHE157 4.6 12.3 1.0 CE2 A:PHE157 4.6 14.7 1.0 HD1 A:HIS166 4.7 0.0 1.0 H A:ASP153 4.9 0.0 1.0 HE2 A:HIS179 4.9 0.0 1.0 HD1 A:HIS151 4.9 0.0 1.0 O A:HOH553 4.9 39.4 1.0 CA A:HIS179 5.0 12.5 1.0

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