Atomistry » Zinc » PDB 2ytt-2z3j » 2yxo
Atomistry »
  Zinc »
    PDB 2ytt-2z3j »
      2yxo »

Zinc in PDB 2yxo: Histidinol Phosphate Phosphatase Complexed with Sulfate

Enzymatic activity of Histidinol Phosphate Phosphatase Complexed with Sulfate

All present enzymatic activity of Histidinol Phosphate Phosphatase Complexed with Sulfate:
3.1.3.15;

Protein crystallography data

The structure of Histidinol Phosphate Phosphatase Complexed with Sulfate, PDB code: 2yxo was solved by R.Omi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.85 / 1.60
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 84.771, 97.190, 74.289, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 22.1

Other elements in 2yxo:

The structure of Histidinol Phosphate Phosphatase Complexed with Sulfate also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Histidinol Phosphate Phosphatase Complexed with Sulfate (pdb code 2yxo). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Histidinol Phosphate Phosphatase Complexed with Sulfate, PDB code: 2yxo:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2yxo

Go back to Zinc Binding Sites List in 2yxo
Zinc binding site 1 out of 2 in the Histidinol Phosphate Phosphatase Complexed with Sulfate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Histidinol Phosphate Phosphatase Complexed with Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:20.8
occ:1.00
NE2 A:HIS38 2.1 19.5 1.0
O3 A:SO42001 2.1 21.4 1.0
NE2 A:HIS13 2.2 20.9 1.0
NE2 A:HIS226 2.2 21.0 1.0
O1 A:SO42001 2.7 22.5 1.0
S A:SO42001 3.0 21.8 1.0
CD2 A:HIS13 3.1 20.9 1.0
CE1 A:HIS38 3.1 18.3 1.0
CD2 A:HIS38 3.1 18.3 1.0
CD2 A:HIS226 3.2 20.9 1.0
CE1 A:HIS13 3.2 19.7 1.0
CE1 A:HIS226 3.2 21.5 1.0
O4 A:SO42001 4.0 20.6 1.0
O2 A:SO42001 4.0 22.4 1.0
CE1 A:HIS7 4.1 18.9 1.0
NE2 A:HIS7 4.2 16.2 1.0
ND1 A:HIS38 4.2 18.0 1.0
ND1 A:HIS7 4.2 17.6 1.0
CG A:HIS38 4.2 17.5 1.0
CG A:HIS13 4.2 20.2 1.0
ND1 A:HIS13 4.3 20.2 1.0
ND1 A:HIS226 4.3 20.9 1.0
CD2 A:HIS7 4.3 18.3 1.0
CG A:HIS226 4.3 20.1 1.0
CG A:HIS7 4.4 17.5 1.0
SG A:CYS11 4.5 18.2 1.0
FE A:FE503 4.6 18.7 1.0

Zinc binding site 2 out of 2 in 2yxo

Go back to Zinc Binding Sites List in 2yxo
Zinc binding site 2 out of 2 in the Histidinol Phosphate Phosphatase Complexed with Sulfate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Histidinol Phosphate Phosphatase Complexed with Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1501

b:20.9
occ:1.00
O2 B:SO42002 2.1 19.5 1.0
O B:HOH2132 2.2 16.9 1.0
OE2 B:GLU80 2.2 18.9 1.0
NE2 B:HIS108 2.2 18.3 1.0
NE2 B:HIS154 2.3 19.3 1.0
CE1 B:HIS108 3.0 19.5 1.0
CD2 B:HIS154 3.1 20.3 1.0
CD B:GLU80 3.1 18.1 1.0
S B:SO42002 3.2 20.4 1.0
CE1 B:HIS154 3.3 21.6 1.0
CD2 B:HIS108 3.3 19.1 1.0
OE1 B:GLU80 3.4 18.6 1.0
FE B:FE1503 3.5 17.4 1.0
O1 B:SO42002 3.5 19.6 1.0
O3 B:SO42002 3.7 20.8 1.0
ND1 B:HIS108 4.2 19.0 1.0
O B:HOH2073 4.2 26.2 1.0
OG B:SER106 4.3 18.8 1.0
CB B:SER106 4.3 18.3 1.0
CG B:HIS154 4.3 19.9 1.0
CG B:HIS108 4.3 19.5 1.0
ND1 B:HIS154 4.4 18.8 1.0
OD2 B:ASP224 4.4 18.6 1.0
CE1 B:HIS38 4.4 17.5 1.0
O4 B:SO42002 4.5 21.5 1.0
CG B:GLU80 4.5 16.7 1.0
CE1 B:HIS5 4.7 18.8 1.0
O B:HOH2070 4.8 27.8 1.0
NE2 B:HIS5 4.8 16.9 1.0
OD2 B:ASP116 4.8 24.1 1.0

Reference:

R.Omi, M.Goto, I.Miyahara, M.Manzoku, A.Ebihara, K.Hirotsu. Crystal Structure of Monofunctional Histidinol Phosphate Phosphatase From Thermus Thermophilus HB8. Biochemistry V. 46 12618 2007.
ISSN: ISSN 0006-2960
PubMed: 17929834
DOI: 10.1021/BI701204R
Page generated: Wed Dec 16 04:03:46 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy