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Manganese in PDB 2o58: Horse Heart Met Manganese Myoglobin

Protein crystallography data

The structure of Horse Heart Met Manganese Myoglobin, PDB code: 2o58 was solved by G.B.Richter-Addo, Z.N.Zahran, L.Chooback, D.M.Copeland, A.H.West, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.47 / 1.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 35.414, 28.654, 62.940, 90.00, 106.01, 90.00
R / Rfree (%) 17.9 / 22.3

Manganese Binding Sites:

The binding sites of Manganese atom in the Horse Heart Met Manganese Myoglobin (pdb code 2o58). 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 Horse Heart Met Manganese Myoglobin, PDB code: 2o58:

Manganese binding site 1 out of 1 in 2o58

Go back to Manganese Binding Sites List in 2o58
Manganese binding site 1 out of 1 in the Horse Heart Met Manganese Myoglobin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Horse Heart Met Manganese Myoglobin within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Mn154

b:13.3
occ:1.00
MN X:MNR154 0.0 13.3 1.0
NC X:MNR154 2.0 10.6 1.0
ND X:MNR154 2.1 10.7 1.0
NA X:MNR154 2.1 11.1 1.0
NB X:MNR154 2.1 13.8 1.0
NE2 X:HIS93 2.2 12.1 1.0
O X:HOH159 2.5 10.3 0.6
C4C X:MNR154 3.0 9.9 1.0
C1C X:MNR154 3.0 6.5 1.0
C1D X:MNR154 3.0 11.6 1.0
C4B X:MNR154 3.0 11.4 1.0
C4A X:MNR154 3.1 7.0 1.0
C4D X:MNR154 3.1 10.9 1.0
C1B X:MNR154 3.1 11.8 1.0
CE1 X:HIS93 3.1 15.5 1.0
C1A X:MNR154 3.1 11.9 1.0
CD2 X:HIS93 3.2 11.6 1.0
CHD X:MNR154 3.4 11.3 1.0
CHC X:MNR154 3.4 7.7 1.0
CHB X:MNR154 3.5 9.2 1.0
CHA X:MNR154 3.5 10.1 1.0
O X:HOH159 4.0 9.2 0.4
ND1 X:HIS93 4.3 14.6 1.0
C3B X:MNR154 4.3 10.3 1.0
C2C X:MNR154 4.3 9.4 1.0
C3C X:MNR154 4.3 12.8 1.0
CG X:HIS93 4.4 12.8 1.0
C2B X:MNR154 4.4 10.3 1.0
C2A X:MNR154 4.4 9.3 1.0
C2D X:MNR154 4.4 12.4 1.0
C3A X:MNR154 4.4 8.8 1.0
C3D X:MNR154 4.4 12.3 1.0
NE2 X:HIS64 4.5 11.7 0.7
NE2 X:HIS64 4.6 9.6 0.3
CG2 X:VAL68 4.7 9.6 1.0
CE1 X:HIS64 4.7 10.4 0.3
CE1 X:HIS64 4.9 12.2 0.7

Reference:

Z.N.Zahran, L.Chooback, D.M.Copeland, A.H.West, G.B.Richter-Addo. Crystal Structures of Manganese- and Cobalt-Substituted Myoglobin in Complex with No and Nitrite Reveal Unusual Ligand Conformations. J.Inorg.Biochem. V. 102 216 2008.
ISSN: ISSN 0162-0134
PubMed: 17905436
DOI: 10.1016/J.JINORGBIO.2007.08.002
Page generated: Tue Dec 15 04:03:53 2020

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