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Manganese in PDB 5lsq: Ethylene Forming Enzyme From Pseudomonas Syringae Pv. Phaseolicola - I222 Crystal Form

Protein crystallography data

The structure of Ethylene Forming Enzyme From Pseudomonas Syringae Pv. Phaseolicola - I222 Crystal Form, PDB code: 5lsq was solved by Z.Zhang, M.A.Mcdonough, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.80 / 1.55
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 79.590, 97.750, 98.550, 90.00, 90.00, 90.00
R / Rfree (%) 13.5 / 15.7

Other elements in 5lsq:

The structure of Ethylene Forming Enzyme From Pseudomonas Syringae Pv. Phaseolicola - I222 Crystal Form also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Ethylene Forming Enzyme From Pseudomonas Syringae Pv. Phaseolicola - I222 Crystal Form (pdb code 5lsq). 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 Ethylene Forming Enzyme From Pseudomonas Syringae Pv. Phaseolicola - I222 Crystal Form, PDB code: 5lsq:

Manganese binding site 1 out of 1 in 5lsq

Go back to Manganese Binding Sites List in 5lsq
Manganese binding site 1 out of 1 in the Ethylene Forming Enzyme From Pseudomonas Syringae Pv. Phaseolicola - I222 Crystal Form


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Ethylene Forming Enzyme From Pseudomonas Syringae Pv. Phaseolicola - I222 Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:8.6
occ:1.00
NE2 A:HIS189 2.0 8.8 1.0
O1 A:B3P403 2.1 13.1 1.0
NE2 A:HIS268 2.1 11.1 1.0
OD1 A:ASP191 2.1 10.9 1.0
O2 A:B3P403 2.1 12.9 1.0
N2 A:B3P403 2.3 13.8 1.0
C8 A:B3P403 2.8 17.2 1.0
C9 A:B3P403 2.9 17.5 1.0
CE1 A:HIS189 3.0 11.3 1.0
C10 A:B3P403 3.0 13.9 1.0
CG A:ASP191 3.0 10.7 1.0
CE1 A:HIS268 3.1 10.1 1.0
CD2 A:HIS268 3.1 9.5 1.0
CD2 A:HIS189 3.1 8.6 1.0
C2 A:B3P403 3.1 16.3 1.0
OD2 A:ASP191 3.2 13.0 1.0
C1 A:B3P403 3.8 20.4 1.0
C3 A:B3P403 4.1 40.9 1.0
ND1 A:HIS189 4.1 10.4 1.0
ND1 A:HIS268 4.2 8.7 1.0
CG A:HIS189 4.2 9.4 1.0
O A:HOH538 4.2 19.2 1.0
CG A:HIS268 4.2 8.8 1.0
C11 A:B3P403 4.3 23.5 1.0
CB A:ASP191 4.4 9.1 1.0
O A:HOH786 4.5 20.5 1.0
O5 A:B3P403 4.6 31.8 1.0
O3 A:B3P403 4.8 24.8 1.0
CA A:ASP191 4.9 9.8 1.0
N A:ASP191 5.0 10.6 1.0

Reference:

Z.Zhang, T.J.Smart, H.Choi, F.Hardy, C.T.Lohans, M.I.Abboud, M.S.W.Richardson, R.S.Paton, M.A.Mcdonough, C.J.Schofield. Structural and Stereoelectronic Insights Into Oxygenase-Catalyzed Formation of Ethylene From 2-Oxoglutarate. Proc. Natl. Acad. Sci. V. 114 4667 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28420789
DOI: 10.1073/PNAS.1617760114
Page generated: Sun Oct 6 01:51:56 2024

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