Calcium in PDB 4yta: Bond Length Analysis of Asp, Glu and His Residues in Trypsin at 1.2A Resolution

All present enzymatic activity of Bond Length Analysis of Asp, Glu and His Residues in Trypsin at 1.2A Resolution:
3.4.21.4;

The structure of Bond Length Analysis of Asp, Glu and His Residues in Trypsin at 1.2A Resolution, PDB code: 4yta was solved by S.J.Fisher, J.R.Helliwell, M.P.Blakeley, M.Cianci, S.Mcsweeny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.45 / 1.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.357, 58.079, 66.899, 90.00, 90.00, 90.00
R / Rfree (%)	10.5 / 12.1

The binding sites of Calcium atom in the Bond Length Analysis of Asp, Glu and His Residues in Trypsin at 1.2A Resolution (pdb code 4yta). 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 Bond Length Analysis of Asp, Glu and His Residues in Trypsin at 1.2A Resolution, PDB code: 4yta:

Calcium binding site 1 out of 1 in the Bond Length Analysis of Asp, Glu and His Residues in Trypsin at 1.2A Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Bond Length Analysis of Asp, Glu and His Residues in Trypsin at 1.2A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca304 b:4.9 occ:1.00 OE1 A:GLU70 2.3 5.4 1.0 O A:VAL75 2.3 5.8 1.0 OE2 A:GLU80 2.3 5.7 1.0 O A:ASN72 2.3 5.5 1.0 O A:HOH599 2.3 7.1 1.0 O A:HOH579 2.4 5.9 1.0 HA A:VAL76 3.3 8.7 1.0 CD A:GLU70 3.3 5.0 1.0 CD A:GLU80 3.4 5.7 1.0 C A:VAL75 3.4 5.6 1.0 HG2 A:GLU80 3.4 7.5 1.0 C A:ASN72 3.5 4.8 1.0 HA A:ILE73 3.5 6.0 0.1 H A:GLU77 3.5 8.8 1.0 HA A:ILE73 3.6 6.1 0.9 H A:VAL75 3.6 6.2 1.0 HG3 A:GLU80 3.7 7.5 1.0 HG3 A:GLU77 3.7 9.9 1.0 CG A:GLU80 3.7 6.2 1.0 OE2 A:GLU70 3.8 5.7 1.0 H A:ASP71 3.8 5.3 1.0 HA A:GLU70 3.9 5.3 1.0 CA A:VAL76 4.1 7.2 1.0 N A:GLU77 4.2 7.3 1.0 HB3 A:ASN72 4.2 7.6 1.0 N A:VAL76 4.2 6.6 1.0 HB2 A:GLU77 4.2 9.5 1.0 N A:VAL75 4.2 5.2 1.0 CA A:ILE73 4.2 5.0 0.1 OE1 A:GLU77 4.3 7.8 1.0 CA A:ILE73 4.3 5.1 0.9 H A:ASN72 4.3 5.3 1.0 N A:ILE73 4.3 5.0 1.0 N A:ASN72 4.4 4.4 1.0 CA A:VAL75 4.4 5.3 1.0 CA A:ASN72 4.5 5.1 1.0 O A:HOH580 4.5 6.7 1.0 CG A:GLU77 4.5 8.3 1.0 HB3 A:GLU70 4.5 5.4 1.0 OE1 A:GLU80 4.5 6.3 1.0 N A:ASP71 4.5 4.5 1.0 C A:ILE73 4.5 5.0 1.0 O A:HOH519 4.6 25.2 1.0 CG A:GLU70 4.6 4.7 1.0 C A:VAL76 4.6 7.5 1.0 HB A:VAL75 4.7 7.2 1.0 CA A:GLU70 4.7 4.4 1.0 CB A:GLU77 4.8 7.9 1.0 CD A:GLU77 4.8 9.1 1.0 CB A:ASN72 4.8 6.3 1.0 CB A:GLU70 4.8 4.5 1.0 N A:ASN74 4.9 4.7 1.0 HG22 A:VAL76 4.9 11.2 1.0 O A:ILE73 4.9 6.2 1.0 H A:ASN74 4.9 5.7 1.0 C A:ASP71 4.9 4.5 1.0 H A:VAL76 5.0 7.9 1.0 HZ A:PHE82 5.0 9.1 1.0 HG2 A:GLU70 5.0 5.6 1.0

S.J.Fisher, M.P.Blakeley, M.Cianci, S.Mcsweeney, J.R.Helliwell. Protonation-State Determination in Proteins Using High-Resolution X-Ray Crystallography: Effects of Resolution and Completeness. Acta Crystallogr.,Sect.D V. 68 800 2012.
ISSN: ISSN 0907-4449
PubMed: 22751665
DOI: 10.1107/S0907444912012589