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Manganese in PDB 3bg3: Crystal Structure of Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus)

Enzymatic activity of Crystal Structure of Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus)

All present enzymatic activity of Crystal Structure of Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus):
6.4.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus), PDB code: 3bg3 was solved by S.Xiang, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 81.274, 173.321, 118.194, 90.00, 95.87, 90.00
R / Rfree (%) 21.6 / 27.1

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus) (pdb code 3bg3). 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 Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus), PDB code: 3bg3:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 3bg3

Go back to Manganese Binding Sites List in 3bg3
Manganese binding site 1 out of 4 in the Crystal Structure of Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus)


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 Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn2001

b:72.0
occ:1.00
OQ1 A:KCX741 2.0 66.8 1.0
OD1 A:ASP572 2.1 59.4 1.0
NE2 A:HIS773 2.2 58.9 1.0
NE2 A:HIS771 2.3 58.3 1.0
OQ2 A:KCX741 2.4 67.2 1.0
CX A:KCX741 2.6 67.1 1.0
CE1 A:HIS771 3.0 58.9 1.0
CG A:ASP572 3.1 58.5 1.0
CE1 A:HIS773 3.2 57.7 1.0
CD2 A:HIS773 3.2 58.7 1.0
OD2 A:ASP572 3.4 58.8 1.0
CD2 A:HIS771 3.4 60.4 1.0
NZ A:KCX741 3.9 67.8 1.0
O3 A:PYR2000 4.2 75.4 1.0
ND1 A:HIS771 4.2 58.9 1.0
ND1 A:HIS773 4.3 57.0 1.0
OE1 A:GLN807 4.3 54.9 1.0
CG A:HIS773 4.3 56.2 1.0
CB A:ASP572 4.4 57.5 1.0
NE2 A:GLN807 4.5 54.5 1.0
CG A:HIS771 4.5 59.7 1.0
NH2 A:ARG571 4.5 55.0 1.0
CA A:MET743 4.8 65.0 1.0
CD A:GLN807 4.8 53.5 1.0
CB A:MET743 5.0 66.0 1.0
CE A:KCX741 5.0 69.6 1.0

Manganese binding site 2 out of 4 in 3bg3

Go back to Manganese Binding Sites List in 3bg3
Manganese binding site 2 out of 4 in the Crystal Structure of Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus)


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 Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn2001

b:69.0
occ:1.00
NE2 B:HIS773 2.2 59.9 1.0
OD1 B:ASP572 2.3 63.5 1.0
OQ1 B:KCX741 2.3 65.5 1.0
OQ2 B:KCX741 2.3 65.5 1.0
NE2 B:HIS771 2.4 59.9 1.0
CX B:KCX741 2.7 65.1 1.0
CE1 B:HIS773 3.1 58.7 1.0
CE1 B:HIS771 3.1 59.3 1.0
CG B:ASP572 3.1 60.0 1.0
OD2 B:ASP572 3.2 61.5 1.0
CD2 B:HIS773 3.3 59.9 1.0
O3 B:PYR2000 3.4 72.9 1.0
CD2 B:HIS771 3.6 62.0 1.0
NZ B:KCX741 4.0 64.9 1.0
OE1 B:GLN807 4.0 58.8 1.0
NH2 B:ARG571 4.2 58.0 1.0
ND1 B:HIS773 4.3 58.5 1.0
ND1 B:HIS771 4.3 60.2 1.0
CG B:HIS773 4.4 59.6 1.0
C2 B:PYR2000 4.5 73.9 1.0
CB B:ASP572 4.5 57.8 1.0
CG B:HIS771 4.6 61.5 1.0
CA B:MET743 4.7 63.8 1.0
C3 B:PYR2000 4.7 74.3 1.0
CE B:KCX741 4.9 66.2 1.0

Manganese binding site 3 out of 4 in 3bg3

Go back to Manganese Binding Sites List in 3bg3
Manganese binding site 3 out of 4 in the Crystal Structure of Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus)


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 Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn2001

b:77.0
occ:1.00
OQ2 C:KCX741 2.1 72.2 1.0
OD1 C:ASP572 2.1 67.2 1.0
NE2 C:HIS773 2.2 63.5 1.0
NE2 C:HIS771 2.3 63.5 1.0
OQ1 C:KCX741 2.8 75.2 1.0
CX C:KCX741 2.8 74.1 1.0
CE1 C:HIS773 2.9 62.0 1.0
CE1 C:HIS771 3.0 63.8 1.0
CG C:ASP572 3.1 66.7 1.0
OD2 C:ASP572 3.2 67.5 1.0
CD2 C:HIS773 3.3 62.5 1.0
CD2 C:HIS771 3.4 64.8 1.0
O3 C:PYR2000 3.9 89.2 1.0
NE2 C:GLN807 4.1 61.2 1.0
NZ C:KCX741 4.1 74.8 1.0
ND1 C:HIS773 4.1 61.6 1.0
ND1 C:HIS771 4.2 64.0 1.0
CG C:HIS773 4.4 61.8 1.0
CG C:HIS771 4.4 65.1 1.0
CB C:ASP572 4.4 65.6 1.0
CA C:MET743 4.5 67.0 1.0
NH1 C:ARG571 4.6 66.2 1.0
CB C:MET743 4.8 68.4 1.0
NH2 C:ARG571 4.8 70.1 1.0
CE C:KCX741 4.9 74.4 1.0
CD C:GLN807 4.9 62.4 1.0

Manganese binding site 4 out of 4 in 3bg3

Go back to Manganese Binding Sites List in 3bg3
Manganese binding site 4 out of 4 in the Crystal Structure of Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus)


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 Human Pyruvate Carboxylase (Missing the Biotin Carboxylase Domain at the N-Terminus) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn2001

b:68.0
occ:1.00
OD1 D:ASP572 2.0 57.4 1.0
OQ2 D:KCX741 2.1 54.1 1.0
NE2 D:HIS771 2.2 55.9 1.0
NE2 D:HIS773 2.4 56.2 1.0
OQ1 D:KCX741 2.6 59.0 1.0
CX D:KCX741 2.7 57.4 1.0
CE1 D:HIS771 3.0 55.6 1.0
CG D:ASP572 3.1 57.5 1.0
CE1 D:HIS773 3.1 55.4 1.0
CD2 D:HIS771 3.4 57.7 1.0
CD2 D:HIS773 3.5 54.8 1.0
OD2 D:ASP572 3.5 58.1 1.0
O3 D:PYR2000 3.8 76.6 1.0
OE1 D:GLN807 4.0 54.5 1.0
NZ D:KCX741 4.1 59.8 1.0
NH2 D:ARG571 4.1 60.2 1.0
ND1 D:HIS771 4.2 56.5 1.0
ND1 D:HIS773 4.3 53.8 1.0
CG D:HIS771 4.4 57.5 1.0
CB D:ASP572 4.4 57.0 1.0
CG D:HIS773 4.5 53.5 1.0
CD D:GLN807 4.8 53.6 1.0
CA D:MET743 4.8 56.3 1.0
CE D:KCX741 5.0 59.5 1.0

Reference:

S.Xiang, L.Tong. Crystal Structures of Human and Staphylococcus Aureus Pyruvate Carboxylase and Molecular Insights Into the Carboxyltransfer Reaction. Nat.Struct.Mol.Biol. V. 15 295 2008.
ISSN: ISSN 1545-9993
PubMed: 18297087
DOI: 10.1038/NSMB.1393
Page generated: Sat Oct 5 15:56:40 2024

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