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Cobalt in PDB 5i8y: Strcuture of Mouse Acireductone Dioxygenase Bound to CO2+ and 2-Keto- 4-(Methylthio)-Butyric Acid

Enzymatic activity of Strcuture of Mouse Acireductone Dioxygenase Bound to CO2+ and 2-Keto- 4-(Methylthio)-Butyric Acid

All present enzymatic activity of Strcuture of Mouse Acireductone Dioxygenase Bound to CO2+ and 2-Keto- 4-(Methylthio)-Butyric Acid:
1.13.11.54;

Protein crystallography data

The structure of Strcuture of Mouse Acireductone Dioxygenase Bound to CO2+ and 2-Keto- 4-(Methylthio)-Butyric Acid, PDB code: 5i8y was solved by A.R.Deshpande, K.Wagenpfeil, T.C.Pochapsky, G.A.Petsko, D.Ringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.11 / 1.94
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.089, 79.089, 115.125, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 19.1

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Strcuture of Mouse Acireductone Dioxygenase Bound to CO2+ and 2-Keto- 4-(Methylthio)-Butyric Acid (pdb code 5i8y). 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 Strcuture of Mouse Acireductone Dioxygenase Bound to CO2+ and 2-Keto- 4-(Methylthio)-Butyric Acid, PDB code: 5i8y:

Cobalt binding site 1 out of 1 in 5i8y

Go back to Cobalt Binding Sites List in 5i8y
Cobalt binding site 1 out of 1 in the Strcuture of Mouse Acireductone Dioxygenase Bound to CO2+ and 2-Keto- 4-(Methylthio)-Butyric Acid


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Strcuture of Mouse Acireductone Dioxygenase Bound to CO2+ and 2-Keto- 4-(Methylthio)-Butyric Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co201

b:22.0
occ:1.00
 OE1 A:GLU94 2.1 22.9 1.0
NE2 A:HIS90 2.1 18.7 1.0
O A:HOH332 2.2 23.7 1.0
NE2 A:HIS88 2.2 21.9 1.0
NE2 A:HIS133 2.2 19.3 1.0
O A:HOH338 2.2 22.1 1.0
CD2 A:HIS90 3.0 20.8 1.0
CD A:GLU94 3.0 23.0 1.0
CE1 A:HIS88 3.1 22.6 1.0
CE1 A:HIS133 3.1 20.2 1.0
CD2 A:HIS133 3.1 20.6 1.0
CE1 A:HIS90 3.2 23.4 1.0
CD2 A:HIS88 3.2 21.1 1.0
OE2 A:GLU94 3.3 24.1 1.0
O2 A:KMT202 4.1 33.6 1.0
O A:HOH395 4.1 23.3 1.0
CG A:HIS90 4.2 25.3 1.0
ND1 A:HIS133 4.2 21.0 1.0
ND1 A:HIS90 4.2 19.5 1.0
O1 A:KMT202 4.2 29.7 1.0
ND1 A:HIS88 4.2 21.8 1.0
CG A:HIS133 4.3 19.9 1.0
CG A:HIS88 4.3 21.1 1.0
O A:HOH486 4.3 25.1 1.0
O A:HOH391 4.3 22.3 1.0
CG A:GLU94 4.4 21.7 1.0
C1 A:KMT202 4.6 31.2 1.0
CB A:GLU94 4.7 19.7 1.0

Reference:

A.R.Deshpande, K.Wagenpfeil, T.C.Pochapsky, G.A.Petsko, D.Ringe. Metal-Dependent Function of A Mammalian Acireductone Dioxygenase. Biochemistry V. 55 1398 2016.
ISSN: ISSN 0006-2960
PubMed: 26858196
DOI: 10.1021/ACS.BIOCHEM.5B01319
Page generated: Tue Jul 30 17:56:44 2024

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