Calcium in PDB 1xug: Trypsin-Babim-Zn+2, pH 8.2

All present enzymatic activity of Trypsin-Babim-Zn+2, pH 8.2:
3.4.21.4;

The structure of Trypsin-Babim-Zn+2, pH 8.2, PDB code: 1xug was solved by B.A.Katz, J.M.Clark, J.S.Finer-Moore, T.E.Jenkins, C.R.Johnson, M.J.Rose, C.Luong, W.R.Moore, R.M.Stroud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.720, 63.500, 68.970, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 22.6

The structure of Trypsin-Babim-Zn+2, pH 8.2 also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Calcium atom in the Trypsin-Babim-Zn+2, pH 8.2 (pdb code 1xug). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Trypsin-Babim-Zn+2, pH 8.2, PDB code: 1xug:

Calcium binding site 1 out of 1 in the Trypsin-Babim-Zn+2, pH 8.2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Trypsin-Babim-Zn+2, pH 8.2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca247 b:24.0 occ:1.00 O A:VAL75 2.2 16.6 1.0 O A:ASN72 2.2 7.7 1.0 O A:HOH248 2.3 10.6 1.0 O A:HOH560 2.3 13.4 1.0 OE1 A:GLU70 2.4 9.4 1.0 OE2 A:GLU80 2.4 12.2 1.0 H1 A:HOH560 3.0 13.9 1.0 H1 A:HOH248 3.0 10.9 1.0 H2 A:HOH248 3.1 11.6 1.0 H2 A:HOH560 3.1 14.2 1.0 HA A:VAL76 3.1 12.6 1.0 C A:VAL75 3.3 13.3 1.0 CD A:GLU70 3.3 10.6 1.0 C A:ASN72 3.4 11.4 1.0 H A:GLU77 3.4 14.6 1.0 H A:VAL75 3.5 16.1 1.0 HG2 A:GLU80 3.5 12.4 1.0 CD A:GLU80 3.5 12.2 1.0 HA A:ILE73 3.5 11.5 1.0 H A:ASP71 3.6 11.1 1.0 HG3 A:GLU77 3.7 16.1 1.0 OE2 A:GLU70 3.7 11.3 1.0 HB3 A:ASN72 3.8 12.5 1.0 CG A:GLU80 3.9 13.1 1.0 CA A:VAL76 4.0 12.5 1.0 HA A:GLU70 4.0 10.5 1.0 H A:ASN72 4.0 13.4 1.0 N A:VAL76 4.0 10.5 1.0 HG3 A:GLU80 4.0 12.6 1.0 N A:VAL75 4.0 14.2 1.0 N A:GLU77 4.2 14.2 1.0 N A:ILE73 4.2 10.2 1.0 CA A:ILE73 4.2 12.5 1.0 CA A:VAL75 4.2 14.4 1.0 N A:ASN72 4.2 13.9 1.0 O A:HOH381 4.2 13.4 1.0 CA A:ASN72 4.3 12.6 1.0 HB A:VAL75 4.4 12.7 1.0 C A:ILE73 4.4 11.5 1.0 OE1 A:GLU77 4.4 15.6 1.0 HB2 A:GLU77 4.5 14.4 1.0 CB A:ASN72 4.5 11.2 1.0 HB3 A:GLU70 4.5 8.5 1.0 OE1 A:GLU80 4.5 12.2 1.0 CG A:GLU77 4.5 15.8 1.0 C A:VAL76 4.6 14.1 1.0 N A:ASP71 4.6 12.8 1.0 CG A:GLU70 4.7 8.5 1.0 N A:ASN74 4.7 14.6 1.0 O A:ILE73 4.8 13.8 1.0 H A:ASN74 4.8 16.6 1.0 HG23 A:VAL76 4.8 13.3 1.0 CA A:GLU70 4.8 7.8 1.0 CB A:GLU70 4.8 9.0 1.0 CB A:VAL75 4.9 12.1 1.0 H1 A:HOH381 4.9 13.5 1.0 CD A:GLU77 4.9 17.9 1.0 CB A:GLU77 4.9 14.4 1.0 H A:VAL76 5.0 12.3 1.0 H2 A:HOH277 5.0 15.2 1.0

B.A.Katz, J.M.Clark, J.S.Finer-Moore, T.E.Jenkins, C.R.Johnson, M.J.Ross, C.Luong, W.R.Moore, R.M.Stroud. Design of Potent Selective Zinc-Mediated Serine Protease Inhibitors. Nature V. 391 608 1998.
ISSN: ISSN 0028-0836
PubMed: 9468142
DOI: 10.1038/35422