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Arsenic in PDB 1qqj: Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution

Enzymatic activity of Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution

All present enzymatic activity of Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution:
3.7.1.2;

Protein crystallography data

The structure of Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution, PDB code: 1qqj was solved by D.E.Timm, H.A.Mueller, P.Bhanumoorthy, J.M.Harp, G.J.Bunick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.10 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 64.000, 109.020, 65.240, 90.00, 95.68, 90.00
R / Rfree (%) 18.3 / 21.1

Other elements in 1qqj:

The structure of Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution (pdb code 1qqj). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution, PDB code: 1qqj:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in 1qqj

Go back to Arsenic Binding Sites List in 1qqj
Arsenic binding site 1 out of 2 in the Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As2004

b:37.6
occ:1.00
AS A:CAC2004 0.0 37.6 1.0
O2 A:CAC2004 1.8 35.3 1.0
O1 A:CAC2004 1.8 33.8 1.0
C2 A:CAC2004 2.0 35.8 1.0
C1 A:CAC2004 2.0 36.1 1.0
OE2 A:GLU199 3.4 15.0 1.0
O A:HOH2068 3.8 47.3 1.0
NZ A:LYS253 3.9 14.3 1.0
NH1 A:ARG237 3.9 17.2 1.0
NE2 A:GLN240 4.0 23.1 1.0
CE1 A:TYR128 4.1 13.6 1.0
NE2 A:HIS133 4.1 13.2 1.0
O A:HOH2072 4.1 19.9 1.0
CD A:GLU199 4.4 14.5 1.0
CE A:LYS253 4.5 15.4 1.0
OH A:TYR128 4.5 14.9 1.0
OE1 A:GLU199 4.6 15.9 1.0
O A:HOH2057 4.7 37.0 1.0
CZ A:TYR128 4.7 14.2 1.0
OE1 A:GLN240 4.8 23.9 1.0
CE1 A:HIS133 4.8 12.9 1.0
CD A:GLN240 4.8 21.4 1.0
CD1 A:TYR128 4.9 13.0 1.0
CZ A:ARG237 5.0 17.5 1.0

Arsenic binding site 2 out of 2 in 1qqj

Go back to Arsenic Binding Sites List in 1qqj
Arsenic binding site 2 out of 2 in the Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As2003

b:37.5
occ:1.00
AS B:CAC2003 0.0 37.5 1.0
O2 B:CAC2003 1.8 34.7 1.0
O1 B:CAC2003 1.8 35.2 1.0
C2 B:CAC2003 2.0 36.3 1.0
C1 B:CAC2003 2.0 36.0 1.0
OE2 B:GLU199 3.4 16.4 1.0
NE2 B:GLN240 3.8 24.5 1.0
NH1 B:ARG237 3.9 18.1 1.0
NZ B:LYS253 3.9 17.2 1.0
NE2 B:HIS133 4.0 13.2 1.0
CE1 B:TYR128 4.0 13.6 1.0
O B:HOH2090 4.2 21.1 1.0
CD B:GLU199 4.3 15.9 1.0
OE1 B:GLU199 4.4 16.4 1.0
CE B:LYS253 4.5 17.0 1.0
OH B:TYR128 4.6 17.5 1.0
CE1 B:HIS133 4.7 13.8 1.0
CZ B:TYR128 4.8 14.3 1.0
CD B:GLN240 4.8 22.9 1.0
CD1 B:TYR128 4.8 12.5 1.0
OE1 B:GLN240 4.9 25.8 1.0
O B:HOH2062 4.9 32.5 1.0
O B:HOH2372 4.9 35.2 1.0
CZ B:ARG237 4.9 18.2 1.0

Reference:

D.E.Timm, H.A.Mueller, P.Bhanumoorthy, J.M.Harp, G.J.Bunick. Crystal Structure and Mechanism of A Carbon-Carbon Bond Hydrolase. Structure Fold.Des. V. 7 1023 1999.
ISSN: ISSN 0969-2126
PubMed: 10508789
DOI: 10.1016/S0969-2126(99)80170-1
Page generated: Tue Oct 27 16:47:16 2020

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