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Magnesium in PDB 3c9h: Crystal Structure of the Substrate Binding Protein of the Abc Transporter From Agrobacterium Tumefaciens

Protein crystallography data

The structure of Crystal Structure of the Substrate Binding Protein of the Abc Transporter From Agrobacterium Tumefaciens, PDB code: 3c9h was solved by R.Zhang, X.Xu, H.Zheng, A.Savchenko, A.M.Edwards, A.Joachimiak, Midwestcenter For Structural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.60 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 75.313, 86.947, 109.642, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 22.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Substrate Binding Protein of the Abc Transporter From Agrobacterium Tumefaciens (pdb code 3c9h). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Substrate Binding Protein of the Abc Transporter From Agrobacterium Tumefaciens, PDB code: 3c9h:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3c9h

Go back to Magnesium Binding Sites List in 3c9h
Magnesium binding site 1 out of 2 in the Crystal Structure of the Substrate Binding Protein of the Abc Transporter From Agrobacterium Tumefaciens


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 Substrate Binding Protein of the Abc Transporter From Agrobacterium Tumefaciens within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:22.3
occ:1.00
O A:SER41 2.3 19.5 1.0
O A:HOH414 2.3 27.2 1.0
OD1 A:ASP43 2.3 21.1 1.0
O7 A:CIT402 2.4 19.1 1.0
O2 A:CIT402 2.5 17.6 1.0
O5 A:CIT402 2.6 18.0 1.0
C1 A:CIT402 3.2 17.9 1.0
C6 A:CIT402 3.2 19.2 1.0
C3 A:CIT402 3.2 17.4 1.0
O A:HOH612 3.4 46.3 1.0
C A:SER41 3.4 19.1 1.0
CG A:ASP43 3.6 23.4 1.0
OH A:TYR238 3.7 21.1 1.0
C2 A:CIT402 3.8 17.5 1.0
O A:HOH521 4.0 33.0 1.0
N A:ASP43 4.0 21.9 1.0
O1 A:CIT402 4.0 17.5 1.0
O A:HOH404 4.1 19.2 1.0
CA A:SER41 4.2 19.0 1.0
OD1 A:ASP67 4.3 31.1 1.0
CE2 A:TYR238 4.3 20.4 1.0
O6 A:CIT402 4.3 19.6 1.0
OD2 A:ASP43 4.3 25.5 1.0
CB A:SER41 4.3 19.0 1.0
CA A:ASP43 4.4 22.2 1.0
CZ A:TYR238 4.5 20.7 1.0
N A:LEU42 4.5 19.2 1.0
C A:LEU42 4.5 20.5 1.0
C4 A:CIT402 4.6 18.1 1.0
CB A:ASP43 4.6 21.6 1.0
CA A:LEU42 4.7 19.8 1.0
O A:HOH502 4.8 36.6 1.0
O4 A:CIT402 4.8 16.9 1.0
OG A:SER41 4.9 18.9 1.0

Magnesium binding site 2 out of 2 in 3c9h

Go back to Magnesium Binding Sites List in 3c9h
Magnesium binding site 2 out of 2 in the Crystal Structure of the Substrate Binding Protein of the Abc Transporter From Agrobacterium Tumefaciens


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 the Substrate Binding Protein of the Abc Transporter From Agrobacterium Tumefaciens within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:22.6
occ:1.00
O B:HOH425 2.3 30.2 1.0
O B:SER41 2.3 18.9 1.0
OD1 B:ASP43 2.4 23.9 1.0
O7 B:CIT402 2.5 20.0 1.0
O1 B:CIT402 2.5 20.8 1.0
O6 B:CIT402 2.6 17.1 1.0
C1 B:CIT402 3.2 19.6 1.0
C6 B:CIT402 3.2 18.8 1.0
C3 B:CIT402 3.3 18.2 1.0
C B:SER41 3.4 18.7 1.0
CG B:ASP43 3.6 23.5 1.0
OH B:TYR238 3.7 20.9 1.0
C2 B:CIT402 3.8 19.0 1.0
O B:HOH487 3.9 33.0 1.0
O2 B:CIT402 4.0 17.8 1.0
N B:ASP43 4.0 20.7 1.0
CA B:SER41 4.2 17.9 1.0
OD1 B:ASP67 4.2 29.6 1.0
O B:HOH414 4.2 23.8 1.0
CE2 B:TYR238 4.3 20.5 1.0
OD2 B:ASP43 4.3 24.1 1.0
O5 B:CIT402 4.4 18.7 1.0
CB B:SER41 4.4 18.4 1.0
CA B:ASP43 4.4 22.0 1.0
N B:LEU42 4.5 18.4 1.0
CZ B:TYR238 4.5 20.1 1.0
C B:LEU42 4.5 19.9 1.0
CB B:ASP43 4.6 21.8 1.0
C4 B:CIT402 4.6 17.0 1.0
CA B:LEU42 4.7 19.1 1.0
O B:HOH500 4.9 38.2 1.0
O3 B:CIT402 4.9 17.2 1.0
OG B:SER41 5.0 17.9 1.0

Reference:

R.Zhang, X.Xu, H.Zheng, A.Savchenko, A.M.Edwards, A.Joachimiak. The Crystal Structure of the Substrate Binding Protein of the Abc Transporter From Agrobacterium Tumefaciens. To Be Published.
Page generated: Mon Dec 14 07:57:08 2020

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