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Manganese in PDB 5yl3: Crystal Structure of Horse Heart Myoglobin Reconstituted with Manganese Porphycene in Resting State at pH 8.5

Protein crystallography data

The structure of Crystal Structure of Horse Heart Myoglobin Reconstituted with Manganese Porphycene in Resting State at pH 8.5, PDB code: 5yl3 was solved by K.Oohora, H.Meichin, Y.Kihira, H.Sugimoto, Y.Shiro, T.Hayashi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 34.575, 28.706, 62.702, 90.00, 106.15, 90.00
R / Rfree (%) 16.8 / 20.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Horse Heart Myoglobin Reconstituted with Manganese Porphycene in Resting State at pH 8.5 (pdb code 5yl3). 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 Horse Heart Myoglobin Reconstituted with Manganese Porphycene in Resting State at pH 8.5, PDB code: 5yl3:

Manganese binding site 1 out of 1 in 5yl3

Go back to Manganese Binding Sites List in 5yl3
Manganese binding site 1 out of 1 in the Crystal Structure of Horse Heart Myoglobin Reconstituted with Manganese Porphycene in Resting State at pH 8.5


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 Horse Heart Myoglobin Reconstituted with Manganese Porphycene in Resting State at pH 8.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:11.4
occ:1.00
MN A:HNN201 0.0 11.4 1.0
NC A:HNN201 2.0 12.3 1.0
NB A:HNN201 2.0 11.1 1.0
ND A:HNN201 2.0 13.5 1.0
NA A:HNN201 2.1 13.2 1.0
NE2 A:HIS93 2.3 8.8 1.0
O A:HOH315 2.4 10.9 0.7
C1D A:HNN201 2.8 14.8 1.0
C4C A:HNN201 2.8 12.1 1.0
C1B A:HNN201 2.8 11.8 1.0
C4A A:HNN201 2.9 15.0 1.0
C4D A:HNN201 3.0 14.3 1.0
C4B A:HNN201 3.1 11.9 1.0
C1C A:HNN201 3.1 13.0 1.0
C1A A:HNN201 3.2 14.0 1.0
CE1 A:HIS93 3.2 9.1 1.0
CD2 A:HIS93 3.3 8.8 1.0
CB1 A:HNN201 3.7 14.4 1.0
CB2 A:HNN201 3.7 13.7 1.0
CD1 A:HNN201 3.8 13.6 1.0
CD2 A:HNN201 3.8 14.1 1.0
C2D A:HNN201 4.1 17.2 1.0
C3C A:HNN201 4.2 13.2 1.0
C2B A:HNN201 4.2 11.7 1.0
C3D A:HNN201 4.2 16.9 1.0
C3A A:HNN201 4.2 16.2 1.0
C2C A:HNN201 4.3 13.4 1.0
C3B A:HNN201 4.3 12.2 1.0
ND1 A:HIS93 4.4 8.9 1.0
CG A:HIS93 4.4 8.9 1.0
C2A A:HNN201 4.4 16.3 1.0
NE2 A:HIS64 4.5 13.1 1.0
CG2 A:VAL68 4.6 8.3 1.0
CE1 A:HIS64 4.7 13.2 1.0

Reference:

K.Oohora, H.Meichin, Y.Kihira, H.Sugimoto, Y.Shiro, T.Hayashi. Manganese(V) Porphycene Complex Responsible For Inert C-H Bond Hydroxylation in A Myoglobin Matrix. J. Am. Chem. Soc. V. 139 18460 2017.
ISSN: ESSN 1520-5126
PubMed: 29237270
DOI: 10.1021/JACS.7B11288
Page generated: Sun Oct 6 03:32:11 2024

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