Atomistry » Magnesium » PDB 7ent-7evi » 7euq
Atomistry »
  Magnesium »
    PDB 7ent-7evi »
      7euq »

Magnesium in PDB 7euq: Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase

Enzymatic activity of Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase

All present enzymatic activity of Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase:
3.5.3.25;

Protein crystallography data

The structure of Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase, PDB code: 7euq was solved by K.Oda, Y.Matoba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.26 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 42.491, 49.755, 60.515, 89.97, 72.2, 89.91
R / Rfree (%) 18.1 / 21.1

Other elements in 7euq:

The structure of Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase also contains other interesting chemical elements:

Manganese (Mn) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase (pdb code 7euq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase, PDB code: 7euq:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 7euq

Go back to Magnesium Binding Sites List in 7euq
Magnesium binding site 1 out of 4 in the Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:32.2
occ:1.00
 O A:HOH594 1.9 33.6 1.0
O A:HOH546 2.0 29.0 1.0
O A:HOH617 2.0 25.6 1.0
O A:HOH614 2.1 37.2 1.0
O A:HOH622 2.1 29.7 1.0
O A:HOH599 2.2 28.9 1.0
O A:HOH541 3.9 20.4 1.0
O A:HOH607 4.0 43.7 1.0
O A:ASN77 4.1 21.8 1.0
O A:HOH618 4.1 36.3 1.0
O A:ASP76 4.1 28.9 1.0
C A:ASP76 4.3 27.2 1.0
O A:HOH548 4.3 25.6 1.0
O A:GLY75 4.3 27.1 1.0
CA A:ASP76 4.5 30.2 1.0
C A:ASN77 4.6 23.9 1.0
O A:LEU234 4.7 22.2 1.0
N A:ASN77 4.8 25.6 1.0
O A:ILE235 4.8 22.8 1.0

Magnesium binding site 2 out of 4 in 7euq

Go back to Magnesium Binding Sites List in 7euq
Magnesium binding site 2 out of 4 in the Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg404

b:22.7
occ:1.00
 O A:HOH575 3.0 39.2 1.0
NE A:ARG59 3.2 19.9 0.6
O A:HOH560 3.3 25.5 1.0
O A:HOH539 3.5 31.5 1.0
CD A:ARG59 3.9 20.2 0.6
CA A:PRO56 4.0 25.4 1.0
NH2 A:ARG59 4.1 20.8 0.6
CZ A:ARG59 4.1 20.1 0.6
CD A:ARG59 4.1 22.2 0.4
CB A:ARG59 4.3 21.9 0.4
CB A:ARG59 4.3 20.8 0.6
CG A:ARG59 4.4 22.4 0.4
O A:PRO56 4.6 26.8 1.0
N A:PRO56 4.7 23.1 1.0
CB A:PRO56 4.7 27.0 1.0
CG A:ARG59 4.7 20.7 0.6
C A:PRO56 4.9 25.4 1.0
O A:LEU55 5.0 23.2 1.0

Magnesium binding site 3 out of 4 in 7euq

Go back to Magnesium Binding Sites List in 7euq
Magnesium binding site 3 out of 4 in the Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg405

b:22.8
occ:1.00
 O B:HOH571 3.0 35.3 1.0
NE B:ARG59 3.1 31.0 1.0
ND2 A:ASN243 3.2 23.0 1.0
O B:HOH560 3.2 24.4 1.0
O B:HOH559 3.4 32.6 1.0
N A:ALA16 3.5 23.8 1.0
CZ3 A:TRP17 3.8 32.4 1.0
CD B:ARG59 3.8 26.5 1.0
CE3 A:TRP17 3.9 28.9 1.0
CA A:ALA15 3.9 23.2 1.0
CB A:ALA15 3.9 25.6 1.0
CZ B:ARG59 4.0 32.5 1.0
NH2 B:ARG59 4.0 32.5 1.0
CA B:PRO56 4.0 23.8 1.0
CG A:ASN243 4.1 21.3 1.0
OD1 A:ASN243 4.1 23.7 1.0
CB A:ALA16 4.1 25.7 1.0
C A:ALA15 4.2 23.9 1.0
CB B:ARG59 4.3 22.1 1.0
CA A:ALA16 4.4 24.0 1.0
O B:PRO56 4.5 23.4 1.0
CB B:PRO56 4.7 25.3 1.0
CG B:ARG59 4.7 24.4 1.0
N B:PRO56 4.7 22.7 1.0
CH2 A:TRP17 4.7 29.7 1.0
C B:PRO56 4.9 23.8 1.0
CD2 A:TRP17 4.9 26.6 1.0
O B:LEU55 4.9 20.1 1.0
N A:TRP17 4.9 21.0 1.0

Magnesium binding site 4 out of 4 in 7euq

Go back to Magnesium Binding Sites List in 7euq
Magnesium binding site 4 out of 4 in the Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of C86H-Y124N-G126H-H196S Mutant of N(Omega)- Hydroxy-L-Arginine Hydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:33.8
occ:1.00
 O B:HOH611 1.9 29.5 1.0
O B:HOH558 2.0 34.5 1.0
O B:HOH618 2.0 30.0 1.0
O B:HOH598 2.1 27.1 1.0
O B:HOH548 2.2 28.4 1.0
O B:HOH610 2.2 36.6 1.0
O B:HOH541 3.9 21.1 1.0
O B:ASN77 4.3 21.7 1.0
O B:HOH538 4.3 23.4 1.0
O B:ASP76 4.4 30.1 1.0
O B:GLY75 4.5 27.6 1.0
C B:ASP76 4.5 27.5 1.0
O B:LEU234 4.6 21.7 1.0
O B:ILE235 4.7 21.3 1.0
CA B:ASP76 4.8 29.3 1.0
C B:ASN77 4.8 21.9 1.0
CA B:ILE235 4.9 21.0 1.0

Reference:

K.Oda, T.Sakaguchi, Y.Matoba. Catalytic Mechanism of Dcsb: Arginase Framework Used For Hydrolyzing Its Inhibitor. Protein Sci. V. 31 E4338 2022.
ISSN: ESSN 1469-896X
PubMed: 35634777
DOI: 10.1002/PRO.4338
Page generated: Wed Oct 2 20:59:49 2024

Last articles

Mg in 5JIC
Mg in 5JDA
Mg in 5JCO
Mg in 5JH7
Mg in 5JD9
Mg in 5JFC
Mg in 5JCB
Mg in 5JCZ
Mg in 5JCP
Mg in 5JCF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy