Atomistry » Manganese » PDB 4gwc-4ilk » 4hnu
Atomistry »
  Manganese »
    PDB 4gwc-4ilk »
      4hnu »

Manganese in PDB 4hnu: Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase

Enzymatic activity of Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase

All present enzymatic activity of Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase:
6.4.1.1;

Protein crystallography data

The structure of Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase, PDB code: 4hnu was solved by L.P.C.Yu, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 3.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 96.569, 258.520, 126.898, 90.00, 109.60, 90.00
R / Rfree (%) 19.4 / 26.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase (pdb code 4hnu). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase, PDB code: 4hnu:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 4hnu

Go back to Manganese Binding Sites List in 4hnu
Manganese binding site 1 out of 4 in the Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1202

b:83.6
occ:1.00
OD1 A:ASP572 2.4 61.3 1.0
NE2 A:HIS771 2.5 56.4 1.0
NE2 A:HIS773 2.5 59.6 1.0
NZ A:LYS741 2.7 53.4 1.0
CE1 A:HIS773 3.3 58.7 1.0
CD2 A:HIS771 3.3 55.4 1.0
CG A:ASP572 3.3 60.2 1.0
CE1 A:HIS771 3.4 54.8 1.0
CD2 A:HIS773 3.7 58.0 1.0
OD2 A:ASP572 3.7 66.8 1.0
CE A:LYS741 4.2 55.4 1.0
ND1 A:HIS771 4.4 52.0 1.0
CG A:HIS771 4.4 53.8 1.0
OE1 A:GLN807 4.5 59.6 1.0
ND1 A:HIS773 4.5 55.5 1.0
CB A:ASP572 4.6 56.9 1.0
NH2 A:ARG571 4.7 55.8 1.0
CG A:HIS773 4.7 52.6 1.0
CG A:LYS741 4.9 51.0 1.0
CA A:MET743 4.9 53.5 1.0
CB A:MET743 4.9 53.3 1.0

Manganese binding site 2 out of 4 in 4hnu

Go back to Manganese Binding Sites List in 4hnu
Manganese binding site 2 out of 4 in the Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1201

b:0.0
occ:1.00
OD1 B:ASP572 2.4 78.9 1.0
NE2 B:HIS773 2.4 86.8 1.0
NE2 B:HIS771 2.5 76.3 1.0
NZ B:LYS741 2.9 70.8 1.0
CE1 B:HIS773 2.9 85.7 1.0
CE1 B:HIS771 3.0 74.6 1.0
CG B:ASP572 3.4 77.2 1.0
CD2 B:HIS771 3.6 77.8 1.0
CD2 B:HIS773 3.7 86.6 1.0
OD2 B:ASP572 3.7 82.9 1.0
ND1 B:HIS771 4.1 73.7 1.0
ND1 B:HIS773 4.2 84.6 1.0
CE B:LYS741 4.2 74.5 1.0
CG B:HIS771 4.5 77.2 1.0
NH2 B:ARG571 4.5 82.1 1.0
CG B:HIS773 4.6 82.1 1.0
CB B:ASP572 4.8 73.0 1.0
NH1 B:ARG571 5.0 83.3 1.0

Manganese binding site 3 out of 4 in 4hnu

Go back to Manganese Binding Sites List in 4hnu
Manganese binding site 3 out of 4 in the Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn1201

b:0.5
occ:1.00
OD1 C:ASP572 2.5 92.4 1.0
NE2 C:HIS771 2.5 77.0 1.0
NE2 C:HIS773 2.6 75.2 1.0
NZ C:LYS741 2.6 74.1 1.0
CE1 C:HIS771 3.1 76.1 1.0
CE1 C:HIS773 3.3 75.2 1.0
CG C:ASP572 3.4 84.9 1.0
OD2 C:ASP572 3.5 87.3 1.0
CD2 C:HIS773 3.7 73.6 1.0
CD2 C:HIS771 3.7 78.3 1.0
CE C:LYS741 4.1 77.7 1.0
ND1 C:HIS771 4.4 76.3 1.0
ND1 C:HIS773 4.5 73.7 1.0
CG C:HIS771 4.7 77.0 1.0
CG C:HIS773 4.7 72.3 1.0
CB C:ASP572 4.8 79.8 1.0
NH2 C:ARG571 4.9 84.9 1.0
CA C:MET743 4.9 80.5 1.0
OE1 C:GLN807 5.0 74.9 1.0

Manganese binding site 4 out of 4 in 4hnu

Go back to Manganese Binding Sites List in 4hnu
Manganese binding site 4 out of 4 in the Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of K442E Mutant of S. Aureus Pyruvate Carboxylase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn1202

b:79.5
occ:1.00
NE2 D:HIS771 2.4 48.6 1.0
OD1 D:ASP572 2.5 58.6 1.0
NE2 D:HIS773 2.7 52.5 1.0
NZ D:LYS741 3.1 48.2 1.0
CE1 D:HIS771 3.2 48.2 1.0
CG D:ASP572 3.3 51.9 1.0
CD2 D:HIS771 3.4 49.8 1.0
OD2 D:ASP572 3.5 58.6 1.0
CE1 D:HIS773 3.5 53.5 1.0
CD2 D:HIS773 3.7 52.8 1.0
ND1 D:HIS771 4.3 50.7 1.0
CG D:HIS771 4.4 48.5 1.0
NH2 D:ARG571 4.5 45.1 1.0
CE D:LYS741 4.6 49.0 1.0
CB D:ASP572 4.6 47.6 1.0
ND1 D:HIS773 4.7 53.3 1.0
CG D:HIS773 4.8 48.8 1.0

Reference:

L.P.Yu, C.Y.Chou, P.H.Choi, L.Tong. Characterizing the Importance of the Biotin Carboxylase Domain Dimer For Staphylococcus Aureus Pyruvate Carboxylase Catalysis. Biochemistry V. 52 488 2013.
ISSN: ISSN 0006-2960
PubMed: 23286247
DOI: 10.1021/BI301294D
Page generated: Tue Dec 15 04:22:00 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy