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Calcium in PDB 7esr: Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase (R32)

Enzymatic activity of Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase (R32)

All present enzymatic activity of Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase (R32):
3.5.3.11;

Protein crystallography data

The structure of Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase (R32), PDB code: 7esr was solved by O.M.Mayans, J.R.Fleming, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.97 / 1.42
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 140.7, 140.7, 95.39, 90, 90, 120
R / Rfree (%) 13.2 / 14.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase (R32) (pdb code 7esr). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase (R32), PDB code: 7esr:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 7esr

Go back to Calcium Binding Sites List in 7esr
Calcium binding site 1 out of 2 in the Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase (R32)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase (R32) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:20.6
occ:1.00
OD1 A:ASP201 2.2 21.4 1.0
OD2 A:ASP295 2.2 23.6 1.0
OD2 A:ASP293 2.2 24.7 1.0
O2 A:EDO503 2.3 31.7 0.9
ND1 A:HIS203 2.3 22.9 1.0
OD1 A:ASP295 2.5 22.7 1.0
O1 A:EDO503 2.6 35.1 0.9
CG A:ASP295 2.7 23.8 1.0
HO2 A:EDO503 2.9 38.1 0.9
CG A:ASP293 3.1 22.0 1.0
CG A:ASP201 3.1 19.9 1.0
HB2 A:HIS203 3.1 25.4 1.0
CA A:CA502 3.2 21.0 1.0
CE1 A:HIS203 3.2 23.6 1.0
C2 A:EDO503 3.3 33.2 0.9
HE1 A:HIS203 3.3 28.3 1.0
HO1 A:EDO503 3.3 42.1 0.9
CG A:HIS203 3.4 22.3 1.0
OD2 A:ASP201 3.5 21.8 1.0
C1 A:EDO503 3.5 34.3 0.9
H21 A:EDO503 3.5 39.8 0.9
OD1 A:ASP293 3.6 21.8 1.0
H A:HIS203 3.7 24.6 1.0
CB A:HIS203 3.7 21.2 1.0
H11 A:EDO503 3.8 41.2 0.9
H A:ARG202 3.8 24.0 1.0
HB3 A:ASP293 3.9 25.0 1.0
CB A:ASP293 4.1 20.9 1.0
HB2 A:TRP307 4.2 26.8 1.0
CB A:ASP295 4.2 19.8 1.0
H22 A:EDO503 4.2 39.8 0.9
N A:HIS203 4.3 20.5 1.0
HB2 A:ASP293 4.3 25.0 1.0
HE3 A:TRP307 4.3 27.0 1.0
NE2 A:HIS203 4.4 21.5 1.0
HG3 A:GLU338 4.4 24.3 1.0
HA A:ASP201 4.4 24.3 1.0
H12 A:EDO503 4.4 41.2 0.9
HB2 A:ARG202 4.4 24.5 1.0
N A:ARG202 4.5 20.0 1.0
CD2 A:HIS203 4.5 22.0 1.0
HB3 A:HIS203 4.5 25.4 1.0
CB A:ASP201 4.5 21.3 1.0
HB3 A:ASP295 4.5 23.8 1.0
HB2 A:ASP295 4.6 23.8 1.0
CA A:HIS203 4.6 20.7 1.0
O A:HOH733 4.7 23.2 1.0
OD2 A:ASP205 4.7 24.5 1.0
OD1 A:ASP205 4.8 27.4 1.0
H A:ASP295 4.8 23.1 1.0
CE3 A:TRP307 4.8 22.5 1.0
CA A:ASP201 4.9 20.3 1.0
HB3 A:ASP201 4.9 25.5 1.0
HB3 A:TRP307 4.9 26.8 1.0
CB A:TRP307 5.0 22.3 1.0

Calcium binding site 2 out of 2 in 7esr

Go back to Calcium Binding Sites List in 7esr
Calcium binding site 2 out of 2 in the Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase (R32)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase (R32) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca502

b:21.0
occ:1.00
HO2 A:EDO503 1.8 38.1 0.9
OD2 A:ASP201 2.0 21.8 1.0
O2 A:EDO503 2.1 31.7 0.9
ND1 A:HIS176 2.1 22.2 1.0
OD2 A:ASP205 2.1 24.5 1.0
OD2 A:ASP293 2.2 24.7 1.0
H21 A:EDO503 2.3 39.8 0.9
C2 A:EDO503 2.5 33.2 0.9
H22 A:EDO503 2.9 39.8 0.9
CG A:ASP201 3.0 19.9 1.0
HB2 A:HIS176 3.0 24.8 1.0
CG A:HIS176 3.0 21.6 1.0
CE1 A:HIS176 3.1 24.9 1.0
HB2 A:ASP293 3.1 25.0 1.0
CA A:CA501 3.2 20.6 1.0
CG A:ASP205 3.2 26.6 1.0
CG A:ASP293 3.2 22.0 1.0
HE2 A:HIS199 3.3 28.1 1.0
HE1 A:HIS176 3.3 29.9 1.0
OD1 A:ASP201 3.3 21.4 1.0
CB A:HIS176 3.4 20.7 1.0
HB3 A:HIS176 3.4 24.8 1.0
OD1 A:ASP205 3.5 27.4 1.0
CB A:ASP293 3.6 20.9 1.0
C1 A:EDO503 3.9 34.3 0.9
HB3 A:ASP293 4.0 25.0 1.0
HB2 A:HIS203 4.0 25.4 1.0
O1 A:EDO503 4.1 35.1 0.9
NE2 A:HIS199 4.1 23.4 1.0
NE2 A:HIS176 4.1 24.8 1.0
HG3 A:GLU338 4.2 24.3 1.0
CD2 A:HIS176 4.2 23.4 1.0
OD1 A:ASP293 4.3 21.8 1.0
CB A:ASP201 4.3 21.3 1.0
HB2 A:ASP201 4.4 25.5 1.0
CB A:ASP205 4.5 24.1 1.0
H11 A:EDO503 4.5 41.2 0.9
H12 A:EDO503 4.6 41.2 0.9
O A:HIS216 4.6 22.8 1.0
O A:HIS203 4.6 22.5 1.0
HG23 A:VAL337 4.6 25.1 1.0
HB2 A:ASP205 4.6 28.9 1.0
HG21 A:VAL337 4.7 25.1 1.0
HB3 A:ASP205 4.7 28.9 1.0
HB3 A:ASP201 4.8 25.5 1.0
CA A:HIS176 4.9 20.5 1.0
HB2 A:HIS216 4.9 23.8 1.0
OE2 A:GLU338 4.9 21.0 1.0
OD2 A:ASP295 4.9 23.6 1.0
HE2 A:HIS176 4.9 29.8 1.0
HE1 A:HIS199 4.9 27.4 1.0
CB A:HIS203 4.9 21.2 1.0
H A:HIS203 4.9 24.6 1.0
HG2 A:GLU338 4.9 24.3 1.0
CG A:GLU338 4.9 20.3 1.0
CE1 A:HIS199 5.0 22.9 1.0
CA A:ASP293 5.0 19.5 1.0
ND1 A:HIS203 5.0 22.9 1.0

Reference:

D.Funck, M.Sinn, J.Fleming, M.Stanoppi, J.Dietrich, R.Lopez-Igual, O.Mayans, J.S.Hartig. Guanidine Hydrolase Is A Novel NI2+-Dependent Enzyme From the Arginase Family Nature 2021.
ISSN: ESSN 1476-4687
Page generated: Fri Jul 19 00:30:09 2024

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