Phosphorus in PDB 1aic: Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal-5'-Phosphate Binding Lysine Residue

Enzymatic activity of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal-5'-Phosphate Binding Lysine Residue

All present enzymatic activity of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal-5'-Phosphate Binding Lysine Residue:
2.6.1.1;

Protein crystallography data

The structure of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal-5'-Phosphate Binding Lysine Residue, PDB code: 1aic was solved by J.Jaeger, J.N.Jansonius, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 87.200, 79.900, 89.600, 90.00, 119.10, 90.00
R / Rfree (%) 19.1 / n/a

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal-5'-Phosphate Binding Lysine Residue (pdb code 1aic). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal-5'-Phosphate Binding Lysine Residue, PDB code: 1aic:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in 1aic

Go back to Phosphorus Binding Sites List in 1aic
Phosphorus binding site 1 out of 2 in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal-5'-Phosphate Binding Lysine Residue


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal-5'-Phosphate Binding Lysine Residue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P411

b:13.8
occ:1.00
 P A:PMP411 0.0 13.8 1.0
O2P A:PMP411 1.5 16.7 1.0
O1P A:PMP411 1.5 12.1 1.0
O3P A:PMP411 1.6 10.3 1.0
O4P A:PMP411 1.6 17.0 1.0
C5A A:PMP411 2.5 18.7 1.0
NH2 A:ARG266 3.5 20.6 1.0
OG1 A:THR109 3.7 15.7 1.0
OG A:SER255 3.8 15.7 1.0
OG A:SER257 3.8 12.3 1.0
N A:GLY108 3.8 12.3 1.0
OH B:TYR70 3.8 10.4 1.0
C5 A:PMP411 3.8 16.1 1.0
NH1 A:ARG266 3.9 7.6 1.0
N A:THR109 4.0 13.4 1.0
CZ A:ARG266 4.1 11.7 1.0
C4A A:PMP411 4.2 17.4 1.0
CA A:GLY108 4.4 12.6 1.0
N4A A:PMP411 4.5 21.9 1.0
C4 A:PMP411 4.5 16.9 1.0
CB A:SER257 4.5 11.8 1.0
C A:GLY108 4.6 16.5 1.0
CE1 B:TYR70 4.6 13.6 1.0
CB A:SER255 4.6 12.5 1.0
C A:GLY107 4.7 11.1 1.0
CZ B:TYR70 4.7 12.1 1.0
CA A:GLY107 4.7 9.5 1.0
CB A:THR109 4.8 14.0 1.0
C6 A:PMP411 4.8 17.6 1.0
CA A:THR109 5.0 15.6 1.0

Phosphorus binding site 2 out of 2 in 1aic

Go back to Phosphorus Binding Sites List in 1aic
Phosphorus binding site 2 out of 2 in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal-5'-Phosphate Binding Lysine Residue


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal-5'-Phosphate Binding Lysine Residue within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P411

b:11.3
occ:1.00
 P B:PMP411 0.0 11.3 1.0
O2P B:PMP411 1.5 16.1 1.0
O1P B:PMP411 1.5 12.2 1.0
O4P B:PMP411 1.5 13.5 1.0
O3P B:PMP411 1.6 8.1 1.0
C5A B:PMP411 2.5 13.7 1.0
N B:GLY108 3.5 17.1 1.0
OG B:SER255 3.6 9.8 1.0
NH2 B:ARG266 3.6 20.8 1.0
OG B:SER257 3.7 11.2 1.0
C5 B:PMP411 3.8 14.0 1.0
N B:THR109 3.9 10.1 1.0
CA B:GLY108 4.0 16.0 1.0
OG1 B:THR109 4.1 15.8 1.0
OH A:TYR70 4.1 8.7 1.0
CB B:SER257 4.3 7.1 1.0
NH1 B:ARG266 4.3 8.7 1.0
C4A B:PMP411 4.3 16.3 1.0
CB B:SER255 4.3 5.8 1.0
C B:GLY107 4.4 14.5 1.0
CZ B:ARG266 4.4 12.7 1.0
C B:GLY108 4.4 14.0 1.0
C4 B:PMP411 4.5 12.0 1.0
CA B:GLY107 4.6 11.5 1.0
C6 B:PMP411 4.7 12.8 1.0
N4A B:PMP411 5.0 19.1 1.0

Reference:

V.N.Malashkevich, J.Jager, M.Ziak, U.Sauder, H.Gehring, P.Christen, J.N.Jansonius. Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal 5'-Phosphate-Binding Lysine Residue. Biochemistry V. 34 405 1995.
ISSN: ISSN 0006-2960
PubMed: 7819232
DOI: 10.1021/BI00002A004
Page generated: Fri Sep 25 12:58:58 2020

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy