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Magnesium in PDB 4n67: Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) with Bound Adp From Bartonella Quintana

Protein crystallography data

The structure of Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) with Bound Adp From Bartonella Quintana, PDB code: 4n67 was solved by Seattle Structural Genomics Center For Infectious Disease, Seattlestructural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.88 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.450, 64.070, 97.600, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 19.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) with Bound Adp From Bartonella Quintana (pdb code 4n67). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) with Bound Adp From Bartonella Quintana, PDB code: 4n67:

Magnesium binding site 1 out of 1 in 4n67

Go back to Magnesium Binding Sites List in 4n67
Magnesium binding site 1 out of 1 in the Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) with Bound Adp From Bartonella Quintana


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 the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) with Bound Adp From Bartonella Quintana within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:27.1
occ:1.00
O2A A:ADP301 2.7 27.7 1.0
N A:ARG154 3.2 12.3 0.5
NH1 A:ARG154 3.2 16.0 0.5
N A:ARG154 3.2 11.5 0.5
O A:HOH647 3.2 46.3 1.0
N A:GLY153 3.4 11.9 1.0
CA A:GLY151 3.5 11.8 1.0
CG A:ARG154 3.5 12.8 0.5
O3B A:ADP301 3.5 25.4 1.0
C A:GLY151 3.6 11.4 1.0
CD A:ARG154 3.6 13.3 0.5
CG A:ARG154 3.7 16.1 0.5
CA A:GLY153 3.7 12.0 1.0
CB A:ARG154 3.8 14.4 0.5
CB A:ARG154 3.8 12.0 0.5
N A:ASN152 3.9 11.2 1.0
O A:GLY151 3.9 11.2 1.0
C A:GLY153 3.9 12.1 1.0
PA A:ADP301 4.0 28.5 1.0
CA A:ARG154 4.1 12.9 0.5
CA A:ARG154 4.1 11.4 0.5
N A:GLY151 4.2 11.9 1.0
CZ A:ARG154 4.2 15.3 0.5
C A:ASN152 4.3 11.0 1.0
NE A:ARG154 4.3 14.7 0.5
CD A:ARG154 4.4 17.7 0.5
PB A:ADP301 4.4 25.5 1.0
NE A:ARG154 4.5 19.5 0.5
O1A A:ADP301 4.6 32.2 1.0
O3A A:ADP301 4.6 29.5 1.0
O2B A:ADP301 4.6 22.5 1.0
NH1 A:ARG157 4.7 19.4 1.0
CA A:ASN152 4.7 11.2 1.0
CZ A:PHE63 4.9 12.3 1.0

Reference:

D.M.Dranow, J Abendroth, T.E.Edwards, D.Lorimer. Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) with Bound Adp From Bartonella Quintana To Be Published.
Page generated: Mon Aug 19 23:26:42 2024

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