Atomistry » Iron » PDB 1q5e-1qom » 1qfc
Atomistry »
  Iron »
    PDB 1q5e-1qom »
      1qfc »

Iron in PDB 1qfc: Structure of Rat Purple Acid Phosphatase

Enzymatic activity of Structure of Rat Purple Acid Phosphatase

All present enzymatic activity of Structure of Rat Purple Acid Phosphatase:
3.1.3.2;

Protein crystallography data

The structure of Structure of Rat Purple Acid Phosphatase, PDB code: 1qfc was solved by J.Uppenberg, F.Lindqvist, C.Svensson, B.Ek-Rylander, G.Andersson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.70
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 116.380, 116.380, 63.270, 90.00, 90.00, 90.00
R / Rfree (%) 23.4 / 28.1

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Rat Purple Acid Phosphatase (pdb code 1qfc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Rat Purple Acid Phosphatase, PDB code: 1qfc:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1qfc

Go back to Iron Binding Sites List in 1qfc
Iron binding site 1 out of 2 in the Structure of Rat Purple Acid Phosphatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Rat Purple Acid Phosphatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:49.6
occ:1.00
OD1 A:ASN91 2.0 35.6 1.0
ND1 A:HIS221 2.1 61.4 1.0
NE2 A:HIS186 2.2 30.0 1.0
OD2 A:ASP52 2.2 69.5 1.0
O2 A:PO4410 2.5 41.1 1.0
CE1 A:HIS221 2.9 52.5 1.0
CG A:ASP52 3.0 67.5 1.0
FE A:FE402 3.1 56.8 1.0
CG A:ASN91 3.1 42.6 1.0
OD1 A:ASP52 3.1 53.2 1.0
CD2 A:HIS186 3.1 35.2 1.0
CE1 A:HIS186 3.1 39.1 1.0
CG A:HIS221 3.3 58.7 1.0
O1 A:PO4410 3.4 41.1 1.0
P A:PO4410 3.4 41.1 1.0
CA A:HIS221 3.6 36.5 1.0
ND2 A:ASN91 3.6 33.2 1.0
OD2 A:ASP14 3.7 43.1 1.0
CB A:HIS221 3.8 52.3 1.0
O A:HIS221 4.0 34.2 1.0
O4 A:PO4410 4.0 41.1 1.0
NE2 A:HIS221 4.1 43.3 1.0
ND1 A:HIS186 4.3 30.9 1.0
CG A:HIS186 4.3 25.3 1.0
C A:HIS221 4.3 36.5 1.0
CD2 A:HIS221 4.3 56.6 1.0
CB A:ASN91 4.4 27.3 1.0
CB A:ASP52 4.5 54.3 1.0
N A:ASN91 4.5 49.3 1.0
CD2 A:HIS92 4.5 42.8 1.0
N A:HIS221 4.6 33.4 1.0
OH A:TYR55 4.7 51.4 1.0
O3 A:PO4410 4.7 41.1 1.0
CG A:ASP14 4.8 47.4 1.0
CE1 A:TYR187 4.9 40.7 1.0

Iron binding site 2 out of 2 in 1qfc

Go back to Iron Binding Sites List in 1qfc
Iron binding site 2 out of 2 in the Structure of Rat Purple Acid Phosphatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Rat Purple Acid Phosphatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe402

b:56.8
occ:1.00
OH A:TYR55 2.0 51.4 1.0
NE2 A:HIS223 2.1 44.5 1.0
OD2 A:ASP52 2.1 69.5 1.0
OD2 A:ASP14 2.2 43.1 1.0
O4 A:PO4410 2.8 41.1 1.0
CZ A:TYR55 2.9 63.0 1.0
CD2 A:HIS223 3.0 42.2 1.0
FE A:FE401 3.1 49.6 1.0
CE1 A:HIS223 3.1 48.3 1.0
CG A:ASP52 3.2 67.5 1.0
CE2 A:TYR55 3.2 68.7 1.0
CG A:ASP14 3.3 47.4 1.0
P A:PO4410 3.5 41.1 1.0
O A:HIS221 3.5 34.2 1.0
O1 A:PO4410 3.5 41.1 1.0
O2 A:PO4410 3.6 41.1 1.0
CB A:ASP14 3.9 44.7 1.0
CB A:ASP52 3.9 54.3 1.0
OD1 A:ASP52 4.1 53.2 1.0
CE1 A:TYR55 4.1 66.7 1.0
CG A:HIS223 4.2 49.6 1.0
ND1 A:HIS223 4.2 46.7 1.0
C A:HIS221 4.3 36.5 1.0
CA A:HIS221 4.3 36.5 1.0
OD1 A:ASP14 4.4 46.6 1.0
NE2 A:HIS186 4.4 30.0 1.0
CE1 A:HIS186 4.5 39.1 1.0
ND1 A:HIS221 4.6 61.4 1.0
CD2 A:TYR55 4.6 71.0 1.0
CD2 A:HIS92 4.7 42.8 1.0
CA A:ASP14 4.8 34.9 1.0
OD1 A:ASN91 4.8 35.6 1.0
O3 A:PO4410 5.0 41.1 1.0
N A:HIS221 5.0 33.4 1.0

Reference:

J.Uppenberg, F.Lindqvist, C.Svensson, B.Ek-Rylander, G.Andersson. Crystal Structure of A Mammalian Purple Acid Phosphatase. J.Mol.Biol. V. 290 201 1999.
ISSN: ISSN 0022-2836
PubMed: 10388567
DOI: 10.1006/JMBI.1999.2896
Page generated: Sat Aug 3 13:24:07 2024

Last articles

W in 8QLN
W in 8RJA
V in 8WTN
Te in 8QLN
Re in 9GHX
Rb in 8Z5C
Ni in 9C0T
Ni in 9C0S
Ni in 9GP1
Ni in 9FYO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy