Atomistry » Zinc » PDB 2yu5-2z4g » 2yxo
Atomistry »
  Zinc »
    PDB 2yu5-2z4g »
      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: Thu Oct 24 10:30:11 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy