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Magnesium in PDB 3euk: Crystal Structure of Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer

Protein crystallography data

The structure of Crystal Structure of Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer, PDB code: 3euk was solved by J.S.Woo, J.H.Lim, H.C.Shin, B.H.Oh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 4.00
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 172.414, 172.414, 491.587, 90.00, 90.00, 120.00
R / Rfree (%) 27.1 / 32.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer (pdb code 3euk). 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 Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer, PDB code: 3euk:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 3euk

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Magnesium binding site 1 out of 4 in the Crystal Structure of Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer


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 Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2011

b:56.8
occ:1.00
OG A:SER72 2.6 0.8 1.0
O1B A:AGS2001 2.7 0.5 1.0
O2G A:AGS2001 2.9 0.5 1.0
O3B A:AGS2001 2.9 0.1 1.0
CB A:SER72 3.3 0.4 1.0
PB A:AGS2001 3.3 0.5 1.0
OG1 C:THR1395 3.5 0.2 1.0
PG A:AGS2001 3.5 0.4 1.0
O1A A:AGS2001 3.6 0.5 1.0
OD1 A:ASP1434 3.6 0.7 1.0
N C:THR1395 3.7 0.5 1.0
O3G A:AGS2001 4.0 1.0 1.0
CB C:SER1394 4.0 0.0 1.0
O3A A:AGS2001 4.1 0.7 1.0
CA C:SER1394 4.3 0.4 1.0
CB C:THR1395 4.3 0.4 1.0
PA A:AGS2001 4.5 0.5 1.0
CA A:SER72 4.5 0.1 1.0
N A:SER72 4.5 0.2 1.0
C C:SER1394 4.5 0.8 1.0
CG A:ASP1434 4.6 0.3 1.0
CA C:THR1395 4.6 1.0 1.0
OD2 A:ASP1434 4.7 0.9 1.0
O2B A:AGS2001 4.7 0.7 1.0
OD1 A:ASN93 4.9 0.1 1.0
OG C:SER1394 4.9 0.4 1.0

Magnesium binding site 2 out of 4 in 3euk

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Magnesium binding site 2 out of 4 in the Crystal Structure of Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer


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 Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2012

b:77.2
occ:1.00
O2G C:AGS2002 2.6 86.9 1.0
OG C:SER72 2.7 87.8 1.0
O1A C:AGS2002 2.7 90.8 1.0
O1B C:AGS2002 2.9 85.6 1.0
CB C:SER72 3.3 86.9 1.0
OG1 A:THR1395 3.3 95.7 1.0
N A:THR1395 3.4 96.9 1.0
CB A:SER1394 3.6 97.0 1.0
PB C:AGS2002 3.7 86.5 1.0
O3B C:AGS2002 3.7 86.2 1.0
PG C:AGS2002 3.8 86.7 1.0
CA A:SER1394 3.9 97.5 1.0
PA C:AGS2002 3.9 89.8 1.0
O3A C:AGS2002 4.0 88.1 1.0
CB A:THR1395 4.1 96.9 1.0
OE1 C:GLN1435 4.2 0.1 1.0
C A:SER1394 4.2 96.6 1.0
OD1 C:ASP1434 4.3 0.0 1.0
CA A:THR1395 4.4 97.1 1.0
OG A:SER1394 4.5 95.9 1.0
O3G C:AGS2002 4.6 86.1 1.0
CA C:SER72 4.7 86.0 1.0
O2A C:AGS2002 4.8 91.5 1.0
OD1 C:ASN93 4.9 0.8 1.0
N C:SER72 5.0 87.0 1.0

Magnesium binding site 3 out of 4 in 3euk

Go back to Magnesium Binding Sites List in 3euk
Magnesium binding site 3 out of 4 in the Crystal Structure of Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer


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 Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg2013

b:29.5
occ:1.00
OG F:SER72 2.4 89.5 1.0
O2G F:AGS2003 2.5 87.2 1.0
O1B F:AGS2003 2.7 91.7 1.0
O3G F:AGS2003 3.1 88.8 1.0
PG F:AGS2003 3.1 87.9 1.0
O3B F:AGS2003 3.3 89.1 1.0
CB F:SER72 3.3 90.7 1.0
OG1 H:THR1395 3.3 75.4 1.0
O1A F:AGS2003 3.4 88.3 1.0
OE1 F:GLN1435 3.4 75.8 1.0
PB F:AGS2003 3.5 90.2 1.0
OD1 F:ASP1434 3.8 88.1 1.0
N H:THR1395 3.9 75.5 1.0
CB H:SER1394 4.0 74.5 1.0
O3A F:AGS2003 4.2 88.8 1.0
OD2 F:ASP1434 4.3 88.3 1.0
CB H:THR1395 4.3 75.7 1.0
OG H:SER1394 4.4 70.9 1.0
PA F:AGS2003 4.4 87.8 1.0
CA H:SER1394 4.4 76.0 1.0
CG F:ASP1434 4.5 87.7 1.0
CA F:SER72 4.5 91.0 1.0
N F:SER72 4.6 92.4 1.0
CD F:GLN1435 4.6 77.5 1.0
C H:SER1394 4.7 75.3 1.0
CA H:THR1395 4.8 75.2 1.0
S1G F:AGS2003 4.8 88.1 1.0
O2B F:AGS2003 4.8 91.5 1.0

Magnesium binding site 4 out of 4 in 3euk

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Magnesium binding site 4 out of 4 in the Crystal Structure of Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer


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 Muke-Mukf(Residues 292-443)-Mukb(Head Domain)- Atpgammas Complex, Asymmetric Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg2014

b:0.9
occ:1.00
OG H:SER72 2.4 78.1 1.0
O2G H:AGS2004 2.5 99.2 1.0
O1B H:AGS2004 2.6 99.5 1.0
O3B H:AGS2004 3.0 99.6 1.0
OG1 F:THR1395 3.2 88.0 1.0
CB H:SER72 3.2 82.0 1.0
PG H:AGS2004 3.3 98.9 1.0
PB H:AGS2004 3.4 99.5 1.0
OD1 H:ASP1434 3.6 84.2 1.0
O1A H:AGS2004 3.7 0.5 1.0
N F:THR1395 3.9 92.9 1.0
O3G H:AGS2004 4.0 98.7 1.0
CB F:THR1395 4.2 89.8 1.0
O3A H:AGS2004 4.2 0.5 1.0
CG2 H:THR94 4.4 0.0 1.0
OD2 H:ASP1434 4.4 84.1 1.0
CG H:ASP1434 4.4 84.0 1.0
CB F:SER1394 4.5 97.4 1.0
CA H:SER72 4.5 83.8 1.0
PA H:AGS2004 4.6 0.8 1.0
N H:SER72 4.6 85.0 1.0
CA F:SER1394 4.7 96.9 1.0
CA F:THR1395 4.7 91.3 1.0
O2B H:AGS2004 4.7 98.8 1.0
S1G H:AGS2004 4.8 0.6 1.0
C F:SER1394 4.8 94.8 1.0
OE1 H:GLN1435 4.9 90.0 1.0

Reference:

J.S.Woo, J.H.Lim, H.C.Shin, M.K.Suh, B.Ku, K.H.Lee, K.Joo, H.Robinson, J.Lee, S.Y.Park, N.C.Ha, B.H.Oh. Structural Studies of A Bacterial Condensin Complex Reveal Atp-Dependent Disruption of Intersubunit Interactions. Cell(Cambridge,Mass.) V. 136 85 2009.
ISSN: ISSN 0092-8674
PubMed: 19135891
DOI: 10.1016/J.CELL.2008.10.050
Page generated: Mon Dec 14 08:07:10 2020

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