Calcium in PDB 1bir: Ribonuclease T1, Phe 100 to Ala Mutant Complexed with 2' Gmp

All present enzymatic activity of Ribonuclease T1, Phe 100 to Ala Mutant Complexed with 2' Gmp:
3.1.27.3;

The structure of Ribonuclease T1, Phe 100 to Ala Mutant Complexed with 2' Gmp, PDB code: 1bir was solved by J.Doumen, M.Gonciarz, I.Zegers, R.Loris, L.Wyns, J.Steyaert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.200, 48.190, 40.160, 90.00, 90.26, 90.00
R / Rfree (%)	18.6 / 24

The binding sites of Calcium atom in the Ribonuclease T1, Phe 100 to Ala Mutant Complexed with 2' Gmp (pdb code 1bir). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Ribonuclease T1, Phe 100 to Ala Mutant Complexed with 2' Gmp, PDB code: 1bir:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Ribonuclease T1, Phe 100 to Ala Mutant Complexed with 2' Gmp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ribonuclease T1, Phe 100 to Ala Mutant Complexed with 2' Gmp within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca900 b:24.3 occ:1.00 O A:HOH647 2.4 28.4 1.0 OD2 A:ASP15 2.5 6.2 1.0 O A:HOH508 2.6 15.0 1.0 OD1 A:ASP15 2.7 8.9 1.0 O A:HOH524 2.8 16.4 1.0 CG A:ASP15 2.9 8.8 1.0 O A:HOH628 3.0 24.8 1.0 CB A:ASP15 4.4 7.8 1.0 O A:HOH633 4.4 28.5 1.0 OG A:SER12 4.5 8.3 1.0 O A:CYS10 4.6 9.4 1.0 O A:HOH536 4.7 22.9 1.0 O A:HOH504 4.8 10.6 1.0 N A:SER12 4.9 8.4 1.0

Calcium binding site 2 out of 2 in the Ribonuclease T1, Phe 100 to Ala Mutant Complexed with 2' Gmp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Ribonuclease T1, Phe 100 to Ala Mutant Complexed with 2' Gmp within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca901 b:18.9 occ:1.00 O B:HOH617 2.4 19.2 1.0 OD2 B:ASP15 2.5 10.2 1.0 OD1 B:ASP15 2.5 12.5 1.0 O B:HOH610 2.6 21.2 1.0 O B:HOH636 2.7 40.6 1.0 CG B:ASP15 2.8 11.7 1.0 CB B:ASP15 4.3 9.9 1.0 O B:CYS10 4.6 9.1 1.0 O B:HOH519 4.6 16.7 1.0 O B:HOH516 4.7 11.9 1.0 O B:HOH570 4.7 21.9 1.0 OG B:SER12 4.7 9.9 1.0 CA B:GLY65 4.8 12.2 1.0 O B:HOH533 4.8 17.1 1.0 N B:SER12 5.0 7.1 1.0

J.Doumen, M.Gonciarz, I.Zegers, R.Loris, L.Wyns, J.Steyaert. A Catalytic Function For the Structurally Conserved Residue Phe 100 of Ribonuclease T1. Protein Sci. V. 5 1523 1996.
ISSN: ISSN 0961-8368
PubMed: 8844843