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Calcium in PDB 3gsp: Ribonuclease T1 Complexed with 2',3'-Cgps + 3'-Gmp, 4 Days

Enzymatic activity of Ribonuclease T1 Complexed with 2',3'-Cgps + 3'-Gmp, 4 Days

All present enzymatic activity of Ribonuclease T1 Complexed with 2',3'-Cgps + 3'-Gmp, 4 Days:
3.1.27.3;

Protein crystallography data

The structure of Ribonuclease T1 Complexed with 2',3'-Cgps + 3'-Gmp, 4 Days, PDB code: 3gsp was solved by I.Zegers, L.Wyns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.280, 51.110, 40.550, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 20.9

Calcium Binding Sites:

The binding sites of Calcium atom in the Ribonuclease T1 Complexed with 2',3'-Cgps + 3'-Gmp, 4 Days (pdb code 3gsp). 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 Ribonuclease T1 Complexed with 2',3'-Cgps + 3'-Gmp, 4 Days, PDB code: 3gsp:

Calcium binding site 1 out of 1 in 3gsp

Go back to Calcium Binding Sites List in 3gsp
Calcium binding site 1 out of 1 in the Ribonuclease T1 Complexed with 2',3'-Cgps + 3'-Gmp, 4 Days


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ribonuclease T1 Complexed with 2',3'-Cgps + 3'-Gmp, 4 Days within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca107

b:37.1
occ:1.00
O A:HOH181 2.2 41.6 1.0
OD2 A:ASP15 2.4 10.9 1.0
O A:HOH126 2.4 22.1 1.0
O A:HOH157 2.5 34.9 1.0
O A:HOH162 2.6 37.8 1.0
O A:HOH149 2.7 32.5 1.0
OD1 A:ASP15 2.7 9.9 1.0
CG A:ASP15 2.9 12.4 1.0
CB A:ASP15 4.3 9.4 1.0
O A:HOH166 4.5 38.4 1.0
O A:CYS10 4.5 11.8 1.0
OG A:SER12 4.5 10.7 1.0
O A:HOH158 4.6 35.7 1.0
N A:SER12 4.9 12.3 1.0
O A:HOH117 4.9 16.9 1.0

Reference:

I.Zegers, R.Loris, G.Dehollander, A.Fattah Haikal, F.Poortmans, J.Steyaert, L.Wyns. Hydrolysis of A Slow Cyclic Thiophosphate Substrate of Rnase T1 Analyzed By Time-Resolved Crystallography. Nat.Struct.Biol. V. 5 280 1998.
ISSN: ISSN 1072-8368
PubMed: 9546218
DOI: 10.1038/NSB0498-280
Page generated: Sat Dec 12 04:13:18 2020

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