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Cobalt in PDB 6isd: Crystal Structure of Arabidopsis Thaliana Hppd Complexed with Sulcotrione

Enzymatic activity of Crystal Structure of Arabidopsis Thaliana Hppd Complexed with Sulcotrione

All present enzymatic activity of Crystal Structure of Arabidopsis Thaliana Hppd Complexed with Sulcotrione:
1.13.11.27;

Protein crystallography data

The structure of Crystal Structure of Arabidopsis Thaliana Hppd Complexed with Sulcotrione, PDB code: 6isd was solved by W.C.Yang, G.F.Yang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.75 / 2.40
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 95.571, 95.571, 198.813, 90.00, 90.00, 90.00
R / Rfree (%) 25.8 / 29.4

Other elements in 6isd:

The structure of Crystal Structure of Arabidopsis Thaliana Hppd Complexed with Sulcotrione also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Arabidopsis Thaliana Hppd Complexed with Sulcotrione (pdb code 6isd). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Crystal Structure of Arabidopsis Thaliana Hppd Complexed with Sulcotrione, PDB code: 6isd:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 6isd

Go back to Cobalt Binding Sites List in 6isd
Cobalt binding site 1 out of 2 in the Crystal Structure of Arabidopsis Thaliana Hppd Complexed with Sulcotrione


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Arabidopsis Thaliana Hppd Complexed with Sulcotrione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co601

b:25.1
occ:1.00
OAB A:5BQ600 1.7 30.8 1.0
O A:HOH708 1.9 22.7 1.0
OAD A:5BQ600 2.0 41.2 1.0
OE2 A:GLU394 2.2 29.6 1.0
NE2 A:HIS308 2.2 23.3 1.0
NE2 A:HIS226 2.7 23.6 1.0
CE1 A:HIS308 3.0 23.8 1.0
CAN A:5BQ600 3.0 26.0 1.0
CD A:GLU394 3.2 24.1 1.0
CAP A:5BQ600 3.2 29.9 1.0
CD2 A:HIS226 3.2 21.6 1.0
CD2 A:HIS308 3.3 21.7 1.0
OE1 A:GLU394 3.5 22.8 1.0
CAT A:5BQ600 3.6 31.6 1.0
CE1 A:HIS226 3.9 25.1 1.0
CAL A:5BQ600 4.1 20.4 1.0
ND1 A:HIS308 4.2 28.8 1.0
CG2 A:VAL228 4.3 14.7 1.0
CG A:HIS308 4.3 20.7 1.0
CB A:ALA310 4.3 18.3 1.0
O A:PHE419 4.3 32.4 1.0
CAS A:5BQ600 4.4 34.5 1.0
CE2 A:PHE381 4.5 23.2 1.0
CG A:GLU394 4.5 20.7 1.0
CG A:HIS226 4.6 23.7 1.0
CZ A:PHE381 4.7 27.8 1.0
CB A:GLU394 4.8 19.1 1.0
CD2 A:PHE419 4.8 23.2 1.0
ND1 A:HIS226 4.8 21.9 1.0

Cobalt binding site 2 out of 2 in 6isd

Go back to Cobalt Binding Sites List in 6isd
Cobalt binding site 2 out of 2 in the Crystal Structure of Arabidopsis Thaliana Hppd Complexed with Sulcotrione


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of Arabidopsis Thaliana Hppd Complexed with Sulcotrione within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co502

b:23.6
occ:1.00
OAB B:5BQ501 1.6 24.6 1.0
OAD B:5BQ501 1.9 40.7 1.0
O B:HOH602 2.0 22.2 1.0
OE2 B:GLU394 2.1 35.1 1.0
NE2 B:HIS308 2.2 21.2 1.0
NE2 B:HIS226 2.3 21.9 1.0
CAN B:5BQ501 3.0 31.2 1.0
CE1 B:HIS308 3.0 23.9 1.0
CD B:GLU394 3.1 28.8 1.0
CAP B:5BQ501 3.1 37.9 1.0
CD2 B:HIS226 3.2 19.1 1.0
CE1 B:HIS226 3.3 23.2 1.0
OE1 B:GLU394 3.3 26.6 1.0
CD2 B:HIS308 3.3 21.7 1.0
CAT B:5BQ501 3.7 34.2 1.0
CAL B:5BQ501 3.9 26.8 1.0
ND1 B:HIS308 4.2 23.6 1.0
CE1 B:PHE381 4.2 22.9 1.0
CAS B:5BQ501 4.3 48.3 1.0
CG B:HIS308 4.4 22.0 1.0
ND1 B:HIS226 4.4 20.7 1.0
CG B:HIS226 4.4 21.2 1.0
CG2 B:VAL228 4.4 15.9 1.0
CB B:ALA310 4.4 21.5 1.0
CG B:GLU394 4.4 23.2 1.0
CZ B:PHE381 4.5 25.6 1.0
O B:PHE419 4.6 30.5 1.0
CB B:GLU394 4.7 21.6 1.0
CD2 B:PHE419 4.9 26.0 1.0
CAK B:5BQ501 5.0 51.5 1.0

Reference:

H.Y.Lin, J.F.Yang, D.W.Wang, G.F.Hao, J.Q.Dong, Y.X.Wang, W.C.Yang, J.W.Wu, C.G.Zhan, G.F.Yang. Molecular Insights Into the Mechanism of 4-Hydroxyphenylpyruvate Dioxygenase Inhibition: Enzyme Kinetics, X-Ray Crystallography and Computational Simulations. Febs J. V. 286 975 2019.
ISSN: ISSN 1742-4658
PubMed: 30632699
DOI: 10.1111/FEBS.14747
Page generated: Sun Dec 13 10:50:20 2020

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