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Cobalt in PDB 4zhn: Crystal Structure of Alkb T208A Mutant Protein in Complex with Co(II), 2-Oxoglutarate, and Methylated Trinucleotide T-Mea-T

Enzymatic activity of Crystal Structure of Alkb T208A Mutant Protein in Complex with Co(II), 2-Oxoglutarate, and Methylated Trinucleotide T-Mea-T

All present enzymatic activity of Crystal Structure of Alkb T208A Mutant Protein in Complex with Co(II), 2-Oxoglutarate, and Methylated Trinucleotide T-Mea-T:
1.14.11.33;

Protein crystallography data

The structure of Crystal Structure of Alkb T208A Mutant Protein in Complex with Co(II), 2-Oxoglutarate, and Methylated Trinucleotide T-Mea-T, PDB code: 4zhn was solved by B.Ergel, B.Yu, S.M.Vorobiev, F.Forouhar, J.F.Hunt, Northeast Structuralgenomics Consortium (Nesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.26 / 1.33
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 41.373, 41.373, 116.569, 90.00, 90.00, 90.00
R / Rfree (%) 11.8 / 14.7

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Alkb T208A Mutant Protein in Complex with Co(II), 2-Oxoglutarate, and Methylated Trinucleotide T-Mea-T (pdb code 4zhn). 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 Crystal Structure of Alkb T208A Mutant Protein in Complex with Co(II), 2-Oxoglutarate, and Methylated Trinucleotide T-Mea-T, PDB code: 4zhn:

Cobalt binding site 1 out of 1 in 4zhn

Go back to Cobalt Binding Sites List in 4zhn
Cobalt binding site 1 out of 1 in the Crystal Structure of Alkb T208A Mutant Protein in Complex with Co(II), 2-Oxoglutarate, and Methylated Trinucleotide T-Mea-T


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Alkb T208A Mutant Protein in Complex with Co(II), 2-Oxoglutarate, and Methylated Trinucleotide T-Mea-T within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co301

b:7.2
occ:1.00
 O2 A:AKG302 2.0 8.3 1.0
NE2 A:HIS187 2.1 6.7 1.0
OD1 A:ASP133 2.1 8.6 1.0
NE2 A:HIS131 2.2 7.4 1.0
O5 A:AKG302 2.2 8.0 1.0
O A:HOH413 2.2 11.0 1.0
C1 A:AKG302 2.8 8.6 1.0
C2 A:AKG302 2.8 8.0 1.0
CG A:ASP133 3.0 8.9 1.0
CD2 A:HIS187 3.0 6.4 1.0
CE1 A:HIS187 3.1 6.8 1.0
CE1 A:HIS131 3.1 7.3 1.0
CD2 A:HIS131 3.1 6.6 1.0
OD2 A:ASP133 3.3 10.4 1.0
O1 A:AKG302 4.0 11.4 1.0
NH2 A:ARG210 4.1 11.2 1.0
ND1 A:HIS187 4.2 7.4 1.0
CG A:HIS187 4.2 6.1 1.0
ND1 A:HIS131 4.2 7.5 1.0
CG A:HIS131 4.3 6.9 1.0
C3 A:AKG302 4.3 8.5 1.0
N1 B:MA7502 4.4 7.4 1.0
CB A:ASP133 4.4 8.3 1.0
CN B:MA7502 4.5 9.2 1.0
O A:HOH468 4.5 13.7 1.0
C2 B:MA7502 4.6 7.7 1.0
CZ2 A:TRP178 4.6 8.2 1.0
C6 B:MA7502 4.8 7.7 1.0
N A:ASP133 4.8 8.2 1.0
C4 A:AKG302 4.9 7.9 1.0
CA A:ASP133 4.9 8.3 1.0
CD2 A:LEU128 5.0 9.9 1.0

Reference:

M.L.Hall, B.Ergel, E.B.Miller, B.Yu, D.Rinaldo, J.F.Hunt, R.Friesner. Dft Studies of the Rate-Limiting Step in the Reaction Cycle of the Fe/2OG Dioxygenase Alkb and Related Experimental Studies To Be Published.
Page generated: Tue Jul 30 17:40:32 2024

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