Atomistry » Cobalt » PDB 7cel-7njg » 7e0x
Atomistry »
  Cobalt »
    PDB 7cel-7njg »
      7e0x »

Cobalt in PDB 7e0x: Crystal Structure of Arabidopsis Thaliana Hppd Complexed with 4- Hydroxyphenylacetic Acid

Enzymatic activity of Crystal Structure of Arabidopsis Thaliana Hppd Complexed with 4- Hydroxyphenylacetic Acid

All present enzymatic activity of Crystal Structure of Arabidopsis Thaliana Hppd Complexed with 4- Hydroxyphenylacetic Acid:
1.13.11.27;

Protein crystallography data

The structure of Crystal Structure of Arabidopsis Thaliana Hppd Complexed with 4- Hydroxyphenylacetic Acid, PDB code: 7e0x was solved by H.Y.Lin, G.F.Yang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.68 / 1.89
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.026, 83.889, 62.753, 90, 99.95, 90
R / Rfree (%) 20.5 / 24.3

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Arabidopsis Thaliana Hppd Complexed with 4- Hydroxyphenylacetic Acid (pdb code 7e0x). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of Arabidopsis Thaliana Hppd Complexed with 4- Hydroxyphenylacetic Acid, PDB code: 7e0x:

Cobalt binding site 1 out of 1 in 7e0x

Go back to Cobalt Binding Sites List in 7e0x
Cobalt binding site 1 out of 1 in the Crystal Structure of Arabidopsis Thaliana Hppd Complexed with 4- Hydroxyphenylacetic Acid


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 4- Hydroxyphenylacetic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co501

b:47.0
occ:0.54
 OE1 A:GLU394 2.3 38.6 1.0
NE2 A:HIS226 2.5 36.2 1.0
NE2 A:HIS308 2.6 36.3 1.0
CE1 A:HIS308 3.2 41.0 1.0
CD A:GLU394 3.3 39.1 1.0
CE1 A:HIS226 3.3 31.5 1.0
O1 A:4HP502 3.5 62.0 1.0
OE2 A:GLU394 3.6 43.8 1.0
CD2 A:HIS226 3.6 36.0 1.0
CD2 A:HIS308 3.7 37.2 1.0
C8 A:4HP502 4.2 58.6 1.0
CG2 A:VAL228 4.3 32.6 1.0
O A:PHE419 4.4 51.0 1.0
CE2 A:PHE381 4.4 38.5 1.0
ND1 A:HIS308 4.5 35.4 1.0
ND1 A:HIS226 4.5 37.1 1.0
CB A:ALA310 4.6 28.5 1.0
CG A:GLU394 4.6 31.1 1.0
CG A:HIS226 4.7 32.8 1.0
CZ A:PHE381 4.7 39.8 1.0
C7 A:4HP502 4.7 52.2 1.0
CG A:HIS308 4.8 34.6 1.0
CB A:GLU394 4.8 30.5 1.0
C2 A:4HP502 4.9 62.1 1.0
CD2 A:PHE419 4.9 40.5 1.0
CB A:PHE419 4.9 43.9 1.0
O2 A:4HP502 5.0 61.0 1.0

Reference:

H.Y.Lin, X.Chen, J.Dong, J.F.Yang, H.Xiao, Y.Ye, L.H.Li, C.G.Zhan, W.C.Yang, G.F.Yang. Rational Redesign of Enzyme Via the Combination of Quantum Mechanics/Molecular Mechanics, Molecular Dynamics, and Structural Biology Study. J.Am.Chem.Soc. V. 143 15674 2021.
ISSN: ESSN 1520-5126
PubMed: 34542283
DOI: 10.1021/JACS.1C06227
Page generated: Tue Jul 30 19:13:55 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy