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Sodium in PDB 3fhx: Crystal Structure of D235A Mutant of Human Pyridoxal Kinase

Enzymatic activity of Crystal Structure of D235A Mutant of Human Pyridoxal Kinase

All present enzymatic activity of Crystal Structure of D235A Mutant of Human Pyridoxal Kinase:
2.7.1.35;

Protein crystallography data

The structure of Crystal Structure of D235A Mutant of Human Pyridoxal Kinase, PDB code: 3fhx was solved by M.K.Safo, A.K.Gandhi, F.N.Musayev, M.Ghatge, M.L.Di Salvo, V.Schirch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.93 / 2.50
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 91.224, 115.422, 168.898, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 26.2

Other elements in 3fhx:

The structure of Crystal Structure of D235A Mutant of Human Pyridoxal Kinase also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of D235A Mutant of Human Pyridoxal Kinase (pdb code 3fhx). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of D235A Mutant of Human Pyridoxal Kinase, PDB code: 3fhx:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 3fhx

Go back to Sodium Binding Sites List in 3fhx
Sodium binding site 1 out of 2 in the Crystal Structure of D235A Mutant of Human Pyridoxal Kinase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of D235A Mutant of Human Pyridoxal Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na402

b:40.1
occ:1.00
O A:HOH392 2.1 68.1 1.0
O A:THR148 2.5 32.8 1.0
OG1 A:THR186 2.5 32.3 1.0
O3B A:ATP407 2.6 61.1 1.0
O1G A:ATP407 3.1 72.1 1.0
OD1 A:ASP113 3.2 46.3 1.0
PG A:ATP407 3.3 72.6 1.0
O2B A:ATP407 3.4 44.9 1.0
PB A:ATP407 3.5 47.3 1.0
C A:THR148 3.5 33.2 1.0
N A:ASN150 3.5 36.2 1.0
C A:PRO149 3.6 36.4 1.0
CB A:THR186 3.6 39.2 1.0
CA A:PRO149 3.7 33.7 1.0
CG2 A:THR186 3.7 35.4 1.0
O3G A:ATP407 3.8 64.4 1.0
OE1 A:GLU153 3.9 46.5 1.0
N A:PRO149 4.1 36.1 1.0
O A:PRO149 4.2 33.9 1.0
CG A:ASP113 4.2 46.6 1.0
CA A:ASN150 4.3 35.2 1.0
O3A A:ATP407 4.4 48.9 1.0
OG1 A:THR148 4.4 28.8 1.0
CB A:ASN150 4.5 34.1 1.0
OD2 A:ASP113 4.5 51.6 1.0
CB A:THR148 4.5 28.4 1.0
CA A:THR148 4.7 30.9 1.0
O1B A:ATP407 4.7 47.2 1.0
O2G A:ATP407 4.8 72.2 1.0
CA A:THR186 4.8 36.3 1.0
N A:THR186 4.9 38.7 1.0
CA A:GLY234 4.9 28.2 1.0
CG A:ASN150 5.0 35.4 1.0

Sodium binding site 2 out of 2 in 3fhx

Go back to Sodium Binding Sites List in 3fhx
Sodium binding site 2 out of 2 in the Crystal Structure of D235A Mutant of Human Pyridoxal Kinase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of D235A Mutant of Human Pyridoxal Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na406

b:27.5
occ:1.00
O B:HOH385 2.4 40.3 1.0
O B:THR148 2.5 36.9 1.0
O3B B:ATP409 2.6 52.7 1.0
OG1 B:THR186 2.7 38.6 1.0
O1G B:ATP409 3.1 60.6 1.0
PG B:ATP409 3.1 61.2 1.0
O3G B:ATP409 3.3 55.1 1.0
N B:ASN150 3.3 27.3 1.0
OD2 B:ASP113 3.4 27.3 1.0
PB B:ATP409 3.4 40.9 1.0
O2B B:ATP409 3.5 38.2 1.0
OE1 B:GLU153 3.6 25.8 1.0
C B:PRO149 3.7 30.4 1.0
C B:THR148 3.7 31.1 1.0
CB B:THR186 3.8 37.1 1.0
CA B:PRO149 3.8 25.2 1.0
CG2 B:THR186 3.9 34.4 1.0
OD1 B:ASP113 4.0 25.9 1.0
CA B:ASN150 4.0 30.8 1.0
CB B:ASN150 4.0 30.4 1.0
CG B:ASP113 4.1 32.4 1.0
N B:PRO149 4.2 27.8 1.0
O B:PRO149 4.4 25.7 1.0
O3A B:ATP409 4.4 35.2 1.0
CG B:ASN150 4.5 29.9 1.0
O1B B:ATP409 4.6 35.5 1.0
O2G B:ATP409 4.6 59.0 1.0
CD B:GLU153 4.6 33.5 1.0
OG1 B:THR148 4.7 29.6 1.0
ND2 B:ASN150 4.7 23.8 1.0
CB B:THR148 4.7 27.8 1.0
CA B:THR148 4.9 27.5 1.0
OE2 B:GLU153 4.9 34.3 1.0

Reference:

A.K.Gandhi, M.S.Ghatge, F.N.Musayev, A.Sease, S.O.Aboagye, M.L.Di Salvo, V.Schirch, M.K.Safo. Kinetic and Structural Studies of the Role of the Active Site Residue ASP235 of Human Pyridoxal Kinase. Biochem.Biophys.Res.Commun. V. 381 12 2009.
ISSN: ISSN 0006-291X
PubMed: 19351586
DOI: 10.1016/J.BBRC.2009.01.170
Page generated: Sun Aug 17 14:50:08 2025

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