Calcium 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:

Zinc

(Zn)

2 atoms

The binding sites of Calcium 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 Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of Fibroblast Collagenase-1 Complexed to A Diphenyl- Ether Sulphone Based Hydroxamic Acid, PDB code: 966c:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 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 Calcium with other atoms in the Ca 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:Ca267 b:3.8 occ:1.00 O A:GLY176 1.9 2.0 1.0 OE1 A:GLU201 2.2 4.9 1.0 O A:ASN180 2.4 9.6 1.0 O A:GLY178 2.4 8.3 1.0 OD1 A:ASP198 2.4 2.8 1.0 OD2 A:ASP175 2.4 3.0 1.0 CD A:GLU201 2.9 5.5 1.0 OE2 A:GLU201 2.9 9.8 1.0 C A:GLY176 3.2 3.9 1.0 CG A:ASP198 3.3 2.7 1.0 C A:ASN180 3.5 3.9 1.0 CG A:ASP175 3.6 3.4 1.0 C A:GLY178 3.6 9.7 1.0 C A:PRO177 3.8 5.0 1.0 H A:ASP175 3.9 0.0 1.0 N A:GLY178 3.9 10.0 1.0 N A:ASN180 3.9 2.8 1.0 N A:GLY176 4.0 3.8 1.0 H A:ASN180 4.1 0.0 1.0 OD2 A:ASP198 4.1 2.0 1.0 H A:GLY178 4.1 0.0 1.0 H A:GLY176 4.1 0.0 1.0 N A:PRO177 4.1 3.0 1.0 OD1 A:ASP175 4.1 4.1 1.0 CA A:PRO177 4.1 5.4 1.0 CB A:ASP198 4.1 2.0 1.0 CA A:GLY176 4.2 3.6 1.0 CA A:ASN180 4.2 4.5 1.0 C A:ASP175 4.2 3.4 1.0 O A:PRO177 4.2 12.3 1.0 C A:GLY179 4.2 3.0 1.0 CG A:GLU201 4.3 4.9 1.0 CA A:GLY178 4.3 9.3 1.0 N A:ASP175 4.5 4.4 1.0 O A:ASP175 4.5 4.2 1.0 N A:LEU181 4.5 2.3 1.0 O A:GLY179 4.6 2.1 1.0 N A:GLY179 4.6 5.6 1.0 CA A:ASP175 4.7 3.8 1.0 CA A:GLY179 4.7 3.9 1.0 CB A:ASP175 4.7 3.8 1.0 CB A:ASN180 4.7 10.0 1.0 CA A:LEU181 4.8 2.0 1.0 O A:HOH363 4.9 9.3 1.0

Calcium binding site 2 out of 3 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 Calcium with other atoms in the Ca 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:Ca268 b:5.8 occ:1.00 O A:ASP158 2.1 4.2 1.0 O A:HOH353 2.2 3.0 1.0 O A:GLY192 2.2 2.0 1.0 O A:HOH310 2.2 2.0 1.0 OD2 A:ASP194 2.4 6.9 1.0 O A:GLY190 2.5 12.7 1.0 H1 A:HOH353 2.8 0.0 1.0 H2 A:HOH353 2.9 0.0 1.0 H1 A:HOH310 2.9 0.0 1.0 H2 A:HOH310 3.0 0.0 1.0 CG A:ASP194 3.3 6.6 1.0 C A:ASP158 3.3 6.3 1.0 C A:GLY192 3.5 8.0 1.0 OD1 A:ASP194 3.5 5.5 1.0 C A:GLY190 3.6 4.9 1.0 H A:MET160 3.7 0.0 1.0 H A:ASP194 4.0 0.0 1.0 O A:GLY188 4.0 7.2 1.0 N A:ASP194 4.1 4.4 1.0 CA A:ASP158 4.1 6.9 1.0 N A:GLY192 4.2 8.9 1.0 C A:ILE191 4.2 9.3 1.0 O A:ALA157 4.2 9.5 1.0 O A:HOH375 4.3 12.3 1.0 N A:GLY190 4.3 6.8 1.0 H1 A:HOH375 4.3 0.0 1.0 N A:ILE159 4.4 7.2 1.0 C A:GLY193 4.4 5.4 1.0 CA A:GLY190 4.4 4.8 1.0 CA A:GLY192 4.4 8.1 1.0 N A:MET160 4.4 10.8 1.0 C A:PRO189 4.4 14.1 1.0 O A:ILE191 4.4 3.8 1.0 N A:GLY193 4.4 5.7 1.0 O A:PRO189 4.4 18.8 1.0 H A:GLY192 4.5 0.0 1.0 N A:ILE191 4.5 9.3 1.0 CB A:ASP194 4.5 4.4 1.0 CA A:GLY193 4.5 6.0 1.0 O A:HOH311 4.6 2.0 1.0 CA A:ILE159 4.6 7.6 1.0 H A:GLY190 4.6 0.0 1.0 CA A:ASP194 4.6 2.2 1.0 CA A:ILE191 4.6 9.6 1.0 CH2 A:TRP109 4.7 8.3 1.0 CG A:MET160 4.8 5.4 1.0 H1 A:HOH309 4.8 0.0 1.0 H2 A:HOH375 4.9 0.0 1.0 C A:ILE159 4.9 6.0 1.0 CB A:MET160 4.9 4.9 1.0 O A:HOH309 5.0 9.2 1.0

Calcium binding site 3 out of 3 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 Calcium with other atoms in the Ca binding site number 3 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:Ca269 b:2.9 occ:1.00 O A:HOH278 2.0 3.0 1.0 O A:GLU201 2.2 3.7 1.0 O A:GLU199 2.3 2.0 1.0 O A:HOH279 2.3 4.4 1.0 OD2 A:ASP124 2.5 8.0 1.0 OE1 A:GLU199 2.6 5.0 1.0 OD1 A:ASP124 2.7 9.5 1.0 H1 A:HOH278 2.7 0.0 1.0 H2 A:HOH278 2.8 0.0 1.0 H1 A:HOH279 2.9 0.0 1.0 CG A:ASP124 2.9 9.3 1.0 H2 A:HOH279 3.1 0.0 1.0 O A:HOH277 3.4 13.4 1.0 C A:GLU201 3.4 2.7 1.0 C A:GLU199 3.4 7.6 1.0 CD A:GLU199 3.6 7.0 1.0 H A:TRP203 3.8 0.0 1.0 CG A:GLU199 3.9 5.4 1.0 H2 A:HOH277 3.9 0.0 1.0 HG1 A:THR122 4.0 0.0 1.0 CD1 A:TRP203 4.1 2.3 1.0 HH21 A:ARG165 4.1 0.0 1.0 CA A:GLU199 4.1 8.0 1.0 N A:GLU201 4.1 3.5 1.0 H1 A:HOH277 4.2 0.0 1.0 H A:GLU201 4.2 0.0 1.0 N A:ARG202 4.2 2.6 1.0 CA A:ARG202 4.2 3.2 1.0 HE1 A:TRP203 4.3 0.0 1.0 OG1 A:THR122 4.3 2.2 1.0 CB A:ASP124 4.4 8.6 1.0 NE1 A:TRP203 4.5 3.9 1.0 N A:ASP200 4.5 2.1 1.0 C A:ASP200 4.5 2.3 1.0 CA A:GLU201 4.5 2.3 1.0 O A:HOH347 4.5 8.3 1.0 O A:HOH346 4.6 8.8 1.0 CB A:GLU199 4.6 6.1 1.0 N A:TRP203 4.7 2.5 1.0 CA A:ASP200 4.7 2.1 1.0 OE2 A:GLU199 4.8 4.9 1.0 H2 A:HOH346 4.9 0.0 1.0 H A:ASP124 4.9 0.0 1.0 NH2 A:ARG165 4.9 11.3 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