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Magnesium in PDB 4otp: Crystal Structure of the Catalytic Domain of the Human RIOK1 Atypical Protein Kinase in Complex with Adp/MG2+

Enzymatic activity of Crystal Structure of the Catalytic Domain of the Human RIOK1 Atypical Protein Kinase in Complex with Adp/MG2+

All present enzymatic activity of Crystal Structure of the Catalytic Domain of the Human RIOK1 Atypical Protein Kinase in Complex with Adp/MG2+:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of the Human RIOK1 Atypical Protein Kinase in Complex with Adp/MG2+, PDB code: 4otp was solved by N.A.Laronde, I.N.Kiburu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.95 / 2.70
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 78.760, 78.760, 110.570, 90.00, 90.00, 120.00
R / Rfree (%) 20.4 / 24.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Catalytic Domain of the Human RIOK1 Atypical Protein Kinase in Complex with Adp/MG2+ (pdb code 4otp). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Catalytic Domain of the Human RIOK1 Atypical Protein Kinase in Complex with Adp/MG2+, PDB code: 4otp:

Magnesium binding site 1 out of 1 in 4otp

Go back to Magnesium Binding Sites List in 4otp
Magnesium binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of the Human RIOK1 Atypical Protein Kinase in Complex with Adp/MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Catalytic Domain of the Human RIOK1 Atypical Protein Kinase in Complex with Adp/MG2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:61.8
occ:1.00
O2A A:ADP501 1.8 0.6 1.0
O A:HOH602 2.1 92.7 1.0
O A:HOH603 2.1 67.3 1.0
OD1 A:ASN329 2.1 83.4 1.0
O3B A:ADP501 2.5 0.5 1.0
OD1 A:PHD341 2.9 72.3 1.0
O A:HOH604 2.9 58.2 1.0
CG A:ASN329 3.2 86.1 1.0
PA A:ADP501 3.2 90.3 1.0
ND2 A:ASN329 3.5 84.6 1.0
CG A:PHD341 3.7 78.8 1.0
CB A:PHD341 3.7 75.9 1.0
PB A:ADP501 3.8 0.2 1.0
OP3 A:PHD341 3.8 0.8 1.0
O3A A:ADP501 3.8 56.4 1.0
O5' A:ADP501 3.9 60.6 1.0
P A:PHD341 4.1 0.9 1.0
O1A A:ADP501 4.4 88.5 1.0
CB A:ASN329 4.5 66.6 1.0
O2B A:ADP501 4.6 0.9 1.0
C5' A:ADP501 4.7 65.0 1.0
O A:PHE328 4.7 89.5 1.0
OD2 A:PHD341 4.8 86.6 1.0
OP1 A:PHD341 4.8 0.7 1.0
O1B A:ADP501 4.9 0.1 1.0
CD1 A:ILE340 4.9 73.8 1.0
CA A:ASN329 4.9 75.2 1.0
CG1 A:ILE340 5.0 70.3 1.0
O3' A:ADP501 5.0 90.7 1.0

Reference:

S.Ferreira-Cerca, I.Kiburu, E.Thomson, N.Laronde, E.Hurt. Dominant RIO1 Kinase/Atpase Catalytic Mutant Induces Trapping of Late Pre-40S Biogenesis Factors in 80S-Like Ribosomes. Nucleic Acids Res. V. 42 8635 2014.
ISSN: ISSN 0305-1048
PubMed: 24948609
DOI: 10.1093/NAR/GKU542
Page generated: Tue Aug 20 00:59:22 2024

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