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Magnesium in PDB 1q9s: Crystal Structure of Riboflavin Kinase with Ternary Product Complex

Enzymatic activity of Crystal Structure of Riboflavin Kinase with Ternary Product Complex

All present enzymatic activity of Crystal Structure of Riboflavin Kinase with Ternary Product Complex:
2.7.1.26;

Protein crystallography data

The structure of Crystal Structure of Riboflavin Kinase with Ternary Product Complex, PDB code: 1q9s was solved by S.Karthikeyan, Q.Zhou, A.L.Osterman, H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.15 / 2.42
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 76.312, 118.789, 37.979, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 26

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Riboflavin Kinase with Ternary Product Complex (pdb code 1q9s). 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 Riboflavin Kinase with Ternary Product Complex, PDB code: 1q9s:

Magnesium binding site 1 out of 1 in 1q9s

Go back to Magnesium Binding Sites List in 1q9s
Magnesium binding site 1 out of 1 in the Crystal Structure of Riboflavin Kinase with Ternary Product Complex


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 Riboflavin Kinase with Ternary Product Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:16.5
occ:1.00
O1P A:FMN401 2.0 18.7 1.0
O1B A:ADP301 2.1 24.1 1.0
O A:THR34 2.2 20.3 1.0
OD1 A:ASN36 2.3 22.7 1.0
O2A A:ADP301 2.4 24.2 1.0
OG1 A:THR34 2.4 20.9 1.0
PB A:ADP301 3.0 26.4 1.0
C A:THR34 3.2 17.8 1.0
CG A:ASN36 3.2 22.4 1.0
O3B A:ADP301 3.3 27.8 1.0
P A:FMN401 3.4 22.4 1.0
PA A:ADP301 3.5 23.0 1.0
CB A:THR34 3.5 19.5 1.0
ND2 A:ASN36 3.6 23.8 1.0
CA A:THR34 3.6 18.5 1.0
O A:HOH502 3.6 13.5 1.0
N A:THR34 3.7 19.4 1.0
O3A A:ADP301 3.7 25.8 1.0
C5' A:ADP301 3.7 20.1 1.0
O3P A:FMN401 3.9 18.3 1.0
OE1 A:GLU86 4.0 23.6 1.0
O5' A:ADP301 4.1 22.7 1.0
N A:ALA35 4.2 18.5 1.0
O2P A:FMN401 4.2 20.1 1.0
N A:ASN36 4.3 19.4 1.0
CB A:ASN36 4.4 20.8 1.0
O2B A:ADP301 4.4 24.3 1.0
O5' A:FMN401 4.5 20.3 1.0
C A:ALA35 4.6 19.3 1.0
CA A:ALA35 4.6 19.6 1.0
CG2 A:THR34 4.7 17.6 1.0
C5' A:FMN401 4.7 22.1 1.0
O1A A:ADP301 4.8 25.7 1.0
CD A:GLU86 4.8 25.6 1.0
CA A:GLY22 4.8 19.7 1.0
CA A:ASN36 4.9 19.7 1.0
C A:PRO33 5.0 21.0 1.0

Reference:

S.Karthikeyan, Q.Zhou, A.L.Osterman, H.Zhang. Ligand Binding-Induced Conformational Changes in Riboflavin Kinase: Structural Basis For the Ordered Mechanism. Biochemistry V. 42 12532 2003.
ISSN: ISSN 0006-2960
PubMed: 14580199
DOI: 10.1021/BI035450T
Page generated: Tue Aug 13 11:13:26 2024

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