Calcium in PDB 1ic6: Structure of A Serine Protease Proteinase K From Tritirachium Album Limber at 0.98 A Resolution

All present enzymatic activity of Structure of A Serine Protease Proteinase K From Tritirachium Album Limber at 0.98 A Resolution:
3.4.21.64;

The structure of Structure of A Serine Protease Proteinase K From Tritirachium Album Limber at 0.98 A Resolution, PDB code: 1ic6 was solved by C.Betzel, S.Gourinath, P.Kumar, P.Kaur, M.Perbandt, S.Eschenburg, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 0.98
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	67.288, 67.288, 106.582, 90.00, 90.00, 90.00
R / Rfree (%)	11.4 / 12.4

The binding sites of Calcium atom in the Structure of A Serine Protease Proteinase K From Tritirachium Album Limber at 0.98 A Resolution (pdb code 1ic6). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of A Serine Protease Proteinase K From Tritirachium Album Limber at 0.98 A Resolution, PDB code: 1ic6:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of A Serine Protease Proteinase K From Tritirachium Album Limber at 0.98 A Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of A Serine Protease Proteinase K From Tritirachium Album Limber at 0.98 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca280 b:5.7 occ:1.00 O A:PRO175 2.4 6.4 1.0 O A:VAL177 2.4 6.6 1.0 O A:HOH304 2.5 6.6 1.0 O A:HOH729 2.5 8.5 1.0 O A:HOH303 2.5 7.9 1.0 OD2 A:ASP200 2.5 5.9 1.0 O A:HOH301 2.6 8.8 1.0 OD1 A:ASP200 2.7 7.2 1.0 CG A:ASP200 2.9 5.9 1.0 C A:PRO175 3.5 6.0 1.0 O A:HOH547 3.6 8.4 1.0 C A:VAL177 3.6 5.1 1.0 H A:THR179 3.7 1.9 1.0 HA A:CYS178 3.7 3.7 1.0 HA A:PRO175 3.9 6.6 1.0 HG A:CYS249 4.1 6.5 1.0 H A:VAL177 4.1 5.8 1.0 N A:VAL177 4.2 5.7 1.0 CA A:PRO175 4.2 6.8 1.0 O A:VAL198 4.2 7.1 1.0 HA A:SER176 4.4 5.7 1.0 CB A:ASP200 4.4 6.0 1.0 C A:SER176 4.4 5.9 1.0 N A:SER176 4.5 5.9 1.0 CA A:CYS178 4.5 5.1 1.0 N A:CYS178 4.5 5.0 1.0 O A:GLU174 4.5 5.7 1.0 CA A:VAL177 4.5 5.4 1.0 O A:HOH546 4.6 20.1 1.0 HG21 A:VAL198 4.6 7.9 1.0 N A:THR179 4.6 4.8 1.0 O A:HOH532 4.6 17.6 1.0 O A:HOH465 4.6 17.1 1.0 O A:HOH315 4.6 8.7 1.0 CA A:SER176 4.7 6.0 1.0 OG1 A:THR179 4.8 5.4 1.0 HB A:THR179 4.8 1.9 1.0 HB2 A:ASP200 4.8 5.7 1.0 HB3 A:ASP200 4.9 5.7 1.0 HG1 A:THR179 4.9 1.9 1.0 SG A:CYS249 5.0 5.9 1.0 O A:SER176 5.0 6.9 1.0 HG22 A:VAL198 5.0 7.9 1.0 HG22 A:VAL177 5.0 5.8 1.0

Calcium binding site 2 out of 2 in the Structure of A Serine Protease Proteinase K From Tritirachium Album Limber at 0.98 A Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of A Serine Protease Proteinase K From Tritirachium Album Limber at 0.98 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca281 b:11.7 occ:0.50 O A:THR16 2.6 14.6 1.0 OD2 A:ASP260 2.7 18.5 1.0 OD1 A:ASP260 2.7 20.4 1.0 O A:HOH589 2.9 28.6 1.0 O A:HOH305 3.0 26.5 1.0 CG A:ASP260 3.0 17.6 1.0 O A:HOH683 3.3 69.3 1.0 O A:HOH655 3.4 41.5 0.5 HB A:THR16 3.7 11.2 1.0 C A:THR16 3.8 11.0 1.0 HA A:SER17 3.9 10.4 1.0 HH21 A:ARG12 3.9 8.5 1.0 O A:HOH633 4.2 38.4 1.0 HB3 A:ASN257 4.2 8.8 1.0 HA A:THR16 4.3 10.7 1.0 HD22 A:ASN257 4.4 8.1 1.0 CB A:ASP260 4.5 16.5 1.0 HB3 A:ASP260 4.5 16.6 1.0 CA A:THR16 4.5 10.1 1.0 CB A:THR16 4.5 11.0 1.0 ND2 A:ASN257 4.6 9.6 1.0 N A:SER17 4.6 10.4 1.0 CA A:SER17 4.6 10.3 1.0 O A:HOH690 4.6 32.7 1.0 NH2 A:ARG12 4.7 9.3 1.0 HB3 A:SER17 4.7 11.4 1.0 HB2 A:ASP260 4.8 16.6 1.0 HD3 A:PRO18 4.8 10.1 1.0 CG A:ASN257 4.9 10.2 1.0 HA A:ASP260 4.9 13.7 1.0 HD21 A:ASN257 4.9 8.1 1.0 HH22 A:ARG12 5.0 8.5 1.0 O A:HOH453 5.0 14.2 1.0

C.Betzel, S.Gourinath, P.Kumar, P.Kaur, M.Perbandt, S.Eschenburg, T.P.Singh. Structure of A Serine Protease Proteinase K From Tritirachium Album Limber at 0.98 A Resolution. Biochemistry V. 40 3080 2001.
ISSN: ISSN 0006-2960
PubMed: 11258922
DOI: 10.1021/BI002538N