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Manganese in PDB 3csb: Crystal Structure of Monobody YSX1/Maltose Binding Protein Fusion Complex

Protein crystallography data

The structure of Crystal Structure of Monobody YSX1/Maltose Binding Protein Fusion Complex, PDB code: 3csb was solved by R.N.Gilbreth, S.Koide, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 98.818, 98.818, 134.619, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 23.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Monobody YSX1/Maltose Binding Protein Fusion Complex (pdb code 3csb). 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 Monobody YSX1/Maltose Binding Protein Fusion Complex, PDB code: 3csb:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 3csb

Go back to Manganese Binding Sites List in 3csb
Manganese binding site 1 out of 4 in the Crystal Structure of Monobody YSX1/Maltose Binding Protein Fusion Complex


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 Monobody YSX1/Maltose Binding Protein Fusion Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1223

b:0.3
occ:1.00
O A:HOH1096 4.6 49.3 1.0
OD1 A:ASN201 4.8 30.3 1.0

Manganese binding site 2 out of 4 in 3csb

Go back to Manganese Binding Sites List in 3csb
Manganese binding site 2 out of 4 in the Crystal Structure of Monobody YSX1/Maltose Binding Protein Fusion Complex


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 Monobody YSX1/Maltose Binding Protein Fusion Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1224

b:64.2
occ:1.00
OE1 A:GLU310 2.2 38.6 1.0
OD1 A:ASP287 2.3 40.3 1.0
CG A:ASP287 3.3 33.0 1.0
CD A:GLU310 3.3 35.1 1.0
CG A:GLU310 3.8 32.5 1.0
O A:SER306 3.9 26.5 1.0
OD2 A:ASP287 3.9 31.6 1.0
CB A:ASP287 4.2 30.4 1.0
C A:SER306 4.4 26.1 1.0
OE2 A:GLU310 4.4 43.6 1.0
CB A:SER306 4.4 25.8 1.0
CA A:SER306 4.9 25.9 1.0
OG A:SER306 5.0 26.1 1.0

Manganese binding site 3 out of 4 in 3csb

Go back to Manganese Binding Sites List in 3csb
Manganese binding site 3 out of 4 in the Crystal Structure of Monobody YSX1/Maltose Binding Protein Fusion Complex


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 Monobody YSX1/Maltose Binding Protein Fusion Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1225

b:84.8
occ:1.00
O A:HOH1193 4.0 54.8 1.0
O A:GLY13 4.0 24.4 1.0
O A:LYS15 4.0 24.5 1.0
CE A:LYS297 4.1 38.5 1.0
CG A:LYS297 4.1 29.9 1.0
CE2 A:TYR17 4.4 23.1 1.0
OD1 A:ASP296 4.6 31.1 1.0
O A:HOH1192 4.7 35.5 1.0
CD A:LYS297 4.7 33.7 1.0
CZ A:TYR17 4.7 25.0 1.0
OH A:TYR17 4.9 24.0 1.0
O A:ASP14 4.9 24.7 1.0
CD2 A:TYR17 4.9 23.9 1.0
C A:ASP14 5.0 25.0 1.0
C A:LYS15 5.0 24.2 1.0

Manganese binding site 4 out of 4 in 3csb

Go back to Manganese Binding Sites List in 3csb
Manganese binding site 4 out of 4 in the Crystal Structure of Monobody YSX1/Maltose Binding Protein Fusion Complex


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 Monobody YSX1/Maltose Binding Protein Fusion Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1226

b:56.8
occ:1.00
O A:ASP236 2.4 27.9 1.0
C A:ASP236 3.4 28.1 1.0
CA A:ASP236 4.2 27.6 1.0
N A:THR237 4.3 30.6 1.0
CB A:ASP236 4.3 26.1 1.0
CA A:THR237 4.3 32.5 1.0
CG A:LYS239 4.4 43.7 1.0
C A:THR237 4.8 35.0 1.0
N A:LYS239 4.8 37.3 1.0
O A:HOH1102 4.9 31.7 1.0

Reference:

R.N.Gilbreth, K.Esaki, A.Koide, S.S.Sidhu, S.Koide. A Dominant Conformational Role For Amino Acid Diversity in Minimalist Protein-Protein Interfaces J.Mol.Biol. V. 381 407 2008.
ISSN: ISSN 0022-2836
PubMed: 18602117
DOI: 10.1016/J.JMB.2008.06.014
Page generated: Tue Dec 15 04:08:34 2020

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