Calcium in PDB 1anb: Anionic Trypsin Mutant with Ser 214 Replaced By Glu

All present enzymatic activity of Anionic Trypsin Mutant with Ser 214 Replaced By Glu:
3.4.21.4;

The structure of Anionic Trypsin Mutant with Ser 214 Replaced By Glu, PDB code: 1anb was solved by R.J.Fletterick, M.E.Mcgrath, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 2.80
Space group	I 2 3
Cell size a, b, c (Å), α, β, γ (°)	124.380, 124.380, 124.380, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Calcium atom in the Anionic Trypsin Mutant with Ser 214 Replaced By Glu (pdb code 1anb). 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 Anionic Trypsin Mutant with Ser 214 Replaced By Glu, PDB code: 1anb:

Calcium binding site 1 out of 1 in the Anionic Trypsin Mutant with Ser 214 Replaced By Glu


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Anionic Trypsin Mutant with Ser 214 Replaced By Glu within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca289 b:5.4 occ:1.00 O A:HOH393 2.1 2.0 1.0 OE1 A:GLU70 2.1 10.7 1.0 OE2 A:GLU80 2.2 9.6 1.0 O A:VAL75 2.2 11.1 1.0 O A:ASN72 2.5 10.9 1.0 OE1 A:GLU77 2.7 21.4 1.0 CD A:GLU70 3.1 7.1 1.0 CD A:GLU80 3.1 16.2 1.0 CG A:GLU80 3.3 10.7 1.0 C A:VAL75 3.4 11.5 1.0 C A:ASN72 3.5 10.4 1.0 CD A:GLU77 3.5 19.9 1.0 OE2 A:GLU70 3.6 10.8 1.0 CG A:GLU77 3.8 21.1 1.0 N A:GLU77 4.1 14.3 1.0 OE1 A:GLU80 4.2 9.4 1.0 N A:LEU76 4.3 12.5 1.0 CA A:LEU76 4.3 13.2 1.0 N A:VAL75 4.3 12.5 1.0 CG A:GLU70 4.3 10.1 1.0 N A:ILE73 4.4 10.8 1.0 N A:ASN72 4.4 10.2 1.0 CA A:VAL75 4.4 11.4 1.0 CA A:ASN72 4.5 10.2 1.0 CA A:GLU70 4.5 9.5 1.0 CA A:ILE73 4.5 9.9 1.0 N A:HIS71 4.5 10.2 1.0 CB A:GLU70 4.6 8.0 1.0 CB A:GLU77 4.7 16.0 1.0 C A:LEU76 4.7 14.3 1.0 C A:ILE73 4.7 11.2 1.0 OE2 A:GLU77 4.7 23.4 1.0 CB A:ASN72 4.8 9.8 1.0 CD2 A:LEU76 4.8 17.0 1.0 CB A:GLU80 4.9 13.7 1.0 O A:HOH411 4.9 3.8 1.0 N A:ASN74 5.0 12.2 1.0

M.E.Mcgrath, J.R.Vasquez, C.S.Craik, A.S.Yang, B.Honig, R.J.Fletterick. Perturbing the Polar Environment of ASP102 in Trypsin: Consequences of Replacing Conserved SER214. Biochemistry V. 31 3059 1992.
ISSN: ISSN 0006-2960
PubMed: 1554694
DOI: 10.1021/BI00127A005