Zinc in PDB 966c: Crystal Structure of Fibroblast Collagenase-1 Complexed to A Diphenyl- Ether Sulphone Based Hydroxamic Acid

The structure of Crystal Structure of Fibroblast Collagenase-1 Complexed to A Diphenyl- Ether Sulphone Based Hydroxamic Acid, PDB code: 966c was solved by B.Lovejoy, A.Welch, S.Carr, C.Luong, C.Broka, R.T.Hendricks, J.Campbell, K.Walker, R.Martin, H.Van Wart, M.F.Browner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	38.480, 56.520, 74.230, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 33

The structure of Crystal Structure of Fibroblast Collagenase-1 Complexed to A Diphenyl- Ether Sulphone Based Hydroxamic Acid also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Zinc atom in the Crystal Structure of Fibroblast Collagenase-1 Complexed to A Diphenyl- Ether Sulphone Based Hydroxamic Acid (pdb code 966c). 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 Collagenase-1 Complexed to A Diphenyl- Ether Sulphone Based Hydroxamic Acid, PDB code: 966c:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Fibroblast Collagenase-1 Complexed to A Diphenyl- Ether Sulphone Based Hydroxamic Acid


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 Collagenase-1 Complexed to A Diphenyl- Ether Sulphone Based Hydroxamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn265 b:2.4 occ:1.00 O31 A:RS21 2.1 3.3 1.0 O33 A:RS21 2.2 4.9 1.0 NE2 A:HIS222 2.2 2.7 1.0 NE2 A:HIS218 2.3 2.0 1.0 NE2 A:HIS228 2.4 6.8 1.0 O A:HOH297 2.8 13.4 1.0 C28 A:RS21 2.8 5.0 1.0 N32 A:RS21 2.9 2.0 1.0 CD2 A:HIS218 3.0 2.8 1.0 HOX A:RS21 3.0 0.0 1.0 CD2 A:HIS228 3.1 2.1 1.0 CD2 A:HIS222 3.2 5.5 1.0 CE1 A:HIS222 3.2 4.4 1.0 H1 A:HOH297 3.3 0.0 1.0 H2 A:HOH297 3.4 0.0 1.0 CE1 A:HIS218 3.4 4.4 1.0 CE1 A:HIS228 3.6 4.8 1.0 HNW A:RS21 3.9 0.0 1.0 H402 A:RS21 4.1 0.0 1.0 CG A:HIS218 4.2 3.8 1.0 OE2 A:GLU219 4.3 2.0 1.0 ND1 A:HIS222 4.4 5.8 1.0 C27 A:RS21 4.4 4.9 1.0 CG A:HIS222 4.4 4.0 1.0 CG A:HIS228 4.4 2.0 1.0 ND1 A:HIS218 4.4 3.6 1.0 H391 A:RS21 4.5 0.0 1.0 C17 A:RS21 4.6 2.5 1.0 C18 A:RS21 4.6 4.2 1.0 ND1 A:HIS228 4.6 2.4 1.0 H17 A:RS21 4.6 0.0 1.0 H18 A:RS21 4.6 0.0 1.0 H2 A:HOH350 4.7 0.0 1.0 O A:HOH351 4.7 6.9 1.0 H272 A:RS21 4.8 0.0 1.0 H1 A:HOH351 4.9 0.0 1.0 C40 A:RS21 4.9 3.3 1.0 H271 A:RS21 4.9 0.0 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Fibroblast Collagenase-1 Complexed to A Diphenyl- Ether Sulphone Based Hydroxamic Acid


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 Collagenase-1 Complexed to A Diphenyl- Ether Sulphone Based Hydroxamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn266 b:5.8 occ:1.00 NE2 A:HIS183 2.0 5.8 1.0 OD1 A:ASP170 2.1 8.4 1.0 ND1 A:HIS196 2.3 2.0 1.0 NE2 A:HIS168 2.3 7.5 1.0 CE1 A:HIS183 2.7 8.8 1.0 CG A:ASP170 2.9 5.6 1.0 CD2 A:HIS168 3.0 6.2 1.0 OD2 A:ASP170 3.0 8.7 1.0 CD2 A:HIS183 3.2 8.2 1.0 CG A:HIS196 3.2 2.0 1.0 CE1 A:HIS196 3.3 2.0 1.0 CB A:HIS196 3.5 2.0 1.0 CE1 A:HIS168 3.5 6.1 1.0 CZ A:PHE185 3.7 5.2 1.0 O A:SER172 3.9 4.5 1.0 ND1 A:HIS183 3.9 8.9 1.0 CG A:HIS183 4.2 8.1 1.0 CG A:HIS168 4.2 7.0 1.0 CB A:ASP170 4.3 7.7 1.0 O A:HOH305 4.3 14.4 1.0 CE1 A:PHE185 4.4 4.2 1.0 H2 A:HOH305 4.4 0.0 1.0 CD2 A:HIS196 4.4 2.0 1.0 NE2 A:HIS196 4.4 2.0 1.0 OG A:SER172 4.5 9.4 1.0 ND1 A:HIS168 4.5 6.6 1.0 O A:HOH304 4.6 11.4 1.0 CE2 A:PHE185 4.6 5.9 1.0 H2 A:HOH304 4.8 0.0 1.0 HD1 A:HIS183 4.8 0.0 1.0 H1 A:HOH370 4.8 0.0 1.0 O A:HOH298 4.8 5.3 1.0 H1 A:HOH305 4.9 0.0 1.0 C A:SER172 4.9 7.3 1.0 CB A:SER172 4.9 7.6 1.0 CA A:HIS196 4.9 6.3 1.0 CE2 A:PHE174 5.0 5.8 1.0

B.Lovejoy, A.R.Welch, S.Carr, C.Luong, C.Broka, R.T.Hendricks, J.A.Campbell, K.A.Walker, R.Martin, H.Van Wart, M.F.Browner. Crystal Structures of Mmp-1 and -13 Reveal the Structural Basis For Selectivity of Collagenase Inhibitors. Nat.Struct.Biol. V. 6 217 1999.
ISSN: ISSN 1072-8368
PubMed: 10074939
DOI: 10.1038/6657