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Manganese in PDB 3dx5: Crystal Structure of the Probable 3-Dhs Dehydratase Asbf Involved in the Petrobactin Synthesis From Bacillus Anthracis

Protein crystallography data

The structure of Crystal Structure of the Probable 3-Dhs Dehydratase Asbf Involved in the Petrobactin Synthesis From Bacillus Anthracis, PDB code: 3dx5 was solved by Y.Kim, N.Maltseva, L.Stols, W.Eschenfeldt, B.F.Pfleger, D.H.Sherman, A.Joachimiak, Midwest Center For Structural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.40 / 2.12
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 134.483, 134.483, 72.806, 90.00, 90.00, 120.00
R / Rfree (%) 14.8 / 17.8

Other elements in 3dx5:

The structure of Crystal Structure of the Probable 3-Dhs Dehydratase Asbf Involved in the Petrobactin Synthesis From Bacillus Anthracis also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Probable 3-Dhs Dehydratase Asbf Involved in the Petrobactin Synthesis From Bacillus Anthracis (pdb code 3dx5). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of the Probable 3-Dhs Dehydratase Asbf Involved in the Petrobactin Synthesis From Bacillus Anthracis, PDB code: 3dx5:

Manganese binding site 1 out of 1 in 3dx5

Go back to Manganese Binding Sites List in 3dx5
Manganese binding site 1 out of 1 in the Crystal Structure of the Probable 3-Dhs Dehydratase Asbf Involved in the Petrobactin Synthesis From Bacillus Anthracis


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 the Probable 3-Dhs Dehydratase Asbf Involved in the Petrobactin Synthesis From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn287

b:13.9
occ:1.00
OE2 A:GLU142 2.1 16.2 1.0
O3 A:DHB289 2.1 15.7 1.0
OD2 A:ASP172 2.1 14.1 1.0
ND1 A:HIS198 2.3 10.8 1.0
OE1 A:GLU253 2.4 15.7 1.0
OE2 A:GLU253 2.4 15.0 1.0
CD A:GLU253 2.7 13.9 1.0
CE1 A:HIS198 3.1 11.6 1.0
CD A:GLU142 3.1 14.3 1.0
C3 A:DHB289 3.2 18.3 1.0
CG A:ASP172 3.3 13.1 1.0
CG A:HIS198 3.4 12.6 1.0
NZ A:LYS200 3.5 8.6 1.0
C2 A:DHB289 3.5 18.3 1.0
OE1 A:GLU142 3.7 14.7 1.0
CB A:HIS198 3.8 11.5 1.0
CB A:ASP172 4.1 11.1 1.0
CG A:GLU142 4.2 13.5 1.0
NE2 A:HIS144 4.2 24.0 1.0
CG A:GLU253 4.2 14.0 1.0
OD1 A:ASP172 4.3 12.5 1.0
NE2 A:HIS198 4.3 10.7 1.0
CD2 A:HIS198 4.4 10.9 1.0
C4 A:DHB289 4.5 20.7 1.0
O A:HOH370 4.5 14.9 1.0
CD2 A:HIS144 4.6 22.4 1.0
CD2 A:HIS175 4.6 12.7 1.0
CE A:LYS200 4.8 12.3 1.0
O4 A:DHB289 4.8 20.4 1.0
C1 A:DHB289 4.9 18.2 1.0
NE2 A:HIS175 4.9 12.3 1.0
CB A:GLU253 4.9 12.2 1.0
ND2 A:ASN170 5.0 14.4 1.0
NH2 A:ARG102 5.0 10.0 1.0

Reference:

B.F.Pfleger, Y.Kim, T.D.Nusca, N.Maltseva, J.Y.Lee, C.M.Rath, J.B.Scaglione, B.K.Janes, E.C.Anderson, N.H.Bergman, P.C.Hanna, A.Joachimiak, D.H.Sherman. Structural and Functional Analysis of Asbf: Origin of the Stealth 3,4-Dihydroxybenzoic Acid Subunit For Petrobactin Biosynthesis. Proc.Natl.Acad.Sci.Usa V. 105 17133 2008.
ISSN: ISSN 0027-8424
PubMed: 18955706
DOI: 10.1073/PNAS.0808118105
Page generated: Sat Oct 5 16:07:13 2024

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