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Gold in PDB 4m2j: Crystal Structure of Plp-Dependent Cyclase Orfr in Complex with Au

Protein crystallography data

The structure of Crystal Structure of Plp-Dependent Cyclase Orfr in Complex with Au, PDB code: 4m2j was solved by C.Y.Chang, Y.C.Liu, S.Y.Lyu, C.C.Wu, T.L.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.95
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 132.813, 132.813, 60.689, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 26.9

Gold Binding Sites:

The binding sites of Gold atom in the Crystal Structure of Plp-Dependent Cyclase Orfr in Complex with Au (pdb code 4m2j). This binding sites where shown within 5.0 Angstroms radius around Gold atom.
In total only one binding site of Gold was determined in the Crystal Structure of Plp-Dependent Cyclase Orfr in Complex with Au, PDB code: 4m2j:

Gold binding site 1 out of 1 in 4m2j

Go back to Gold Binding Sites List in 4m2j
Gold binding site 1 out of 1 in the Crystal Structure of Plp-Dependent Cyclase Orfr in Complex with Au


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 1 of Crystal Structure of Plp-Dependent Cyclase Orfr in Complex with Au within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Au402

b:66.3
occ:1.00
ND1 A:HIS117 2.3 65.2 1.0
ND1 A:HIS121 2.5 84.9 1.0
CG A:HIS121 3.0 85.9 1.0
CG A:HIS117 3.1 69.2 1.0
CB A:HIS121 3.2 80.5 1.0
CE1 A:HIS117 3.3 67.8 1.0
CB A:HIS117 3.3 69.9 1.0
CE1 A:HIS121 3.5 91.0 1.0
N A:SER118 3.6 69.7 1.0
C A:HIS117 3.7 70.3 1.0
CA A:SER118 3.8 72.5 1.0
CG A:PRO12 4.0 98.6 1.0
CD2 A:HIS121 4.1 92.9 1.0
CA A:HIS117 4.1 70.9 1.0
O A:HIS117 4.2 75.5 1.0
CD2 A:HIS117 4.2 72.3 1.0
NE2 A:HIS121 4.3 97.7 1.0
NE2 A:HIS117 4.3 71.8 1.0
CB A:SER118 4.3 75.2 1.0
CA A:HIS121 4.5 77.5 1.0
CB A:PRO12 4.7 98.3 1.0

Reference:

C.Y.Chang, S.Y.Lyu, Y.C.Liu, N.S.Hsu, C.C.Wu, C.F.Tang, K.H.Lin, J.Y.Ho, C.J.Wu, M.D.Tsai, T.L.Li. Biosynthesis of Streptolidine Involved Two Unexpected Intermediates Produced By A Dihydroxylase and A Cyclase Through Unusual Mechanisms. Angew.Chem.Int.Ed.Engl. V. 53 1943 2014.
ISSN: ISSN 1433-7851
PubMed: 24505011
DOI: 10.1002/ANIE.201307989
Page generated: Sat Dec 12 01:54:06 2020

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