Phosphorus in PDB 1a3g: Branched-Chain Amino Acid Aminotransferase From Escherichia Coli

All present enzymatic activity of Branched-Chain Amino Acid Aminotransferase From Escherichia Coli:
2.6.1.42;

The structure of Branched-Chain Amino Acid Aminotransferase From Escherichia Coli, PDB code: 1a3g was solved by K.Okada, K.Hirotsu, M.Sato, H.Hayashi, H.Kagamiyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	135.100, 144.000, 102.900, 90.00, 136.10, 90.00
R / Rfree (%)	18.8 / 25.8

The binding sites of Phosphorus atom in the Branched-Chain Amino Acid Aminotransferase From Escherichia Coli (pdb code 1a3g). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 3 binding sites of Phosphorus where determined in the Branched-Chain Amino Acid Aminotransferase From Escherichia Coli, PDB code: 1a3g:
Jump to Phosphorus binding site number: 1; 2; 3;

Phosphorus binding site 1 out of 3 in the Branched-Chain Amino Acid Aminotransferase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Branched-Chain Amino Acid Aminotransferase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:P413 b:22.4 occ:1.00 P A:PLP413 0.0 22.4 1.0 O1P A:PLP413 1.4 22.0 1.0 O3P A:PLP413 1.4 23.1 1.0 O4P A:PLP413 1.6 20.2 1.0 O2P A:PLP413 1.6 21.7 1.0 C5A A:PLP413 2.6 19.4 1.0 O A:HOH1598 3.5 42.9 1.0 N A:ILE220 3.6 23.2 1.0 OG1 A:THR221 3.6 24.0 1.0 OG1 A:THR257 3.6 23.4 1.0 N A:THR257 3.8 24.6 1.0 CA A:GLY219 3.9 22.0 1.0 C5 A:PLP413 4.0 17.9 1.0 NH2 A:ARG59 4.1 12.8 1.0 N A:THR221 4.1 27.0 1.0 C A:GLY219 4.2 22.2 1.0 CA A:GLY256 4.3 22.1 1.0 NH1 A:ARG59 4.3 18.2 1.0 CA A:ILE220 4.5 22.8 1.0 C A:GLY256 4.5 23.4 1.0 CB A:THR221 4.5 25.6 1.0 C4A A:PLP413 4.6 16.7 1.0 CB A:THR257 4.6 23.6 1.0 CB A:ILE220 4.6 21.4 1.0 CZ A:ARG59 4.7 18.1 1.0 CA A:THR257 4.7 26.1 1.0 C4 A:PLP413 4.7 18.7 1.0 NE2 A:HIS56 4.8 21.6 1.0 C A:ILE220 4.8 25.3 1.0 C6 A:PLP413 4.9 16.6 1.0 O A:HOH1732 4.9 48.4 1.0 CA A:THR221 5.0 25.3 1.0

Phosphorus binding site 2 out of 3 in the Branched-Chain Amino Acid Aminotransferase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Branched-Chain Amino Acid Aminotransferase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:P413 b:20.0 occ:1.00 P B:PLP413 0.0 20.0 1.0 O1P B:PLP413 1.4 21.2 1.0 O3P B:PLP413 1.4 24.0 1.0 O4P B:PLP413 1.5 20.6 1.0 O2P B:PLP413 1.6 19.8 1.0 C5A B:PLP413 2.5 21.5 1.0 N B:ILE220 3.5 17.7 1.0 OG1 B:THR257 3.7 23.3 1.0 O B:HOH1565 3.8 25.2 1.0 C5 B:PLP413 3.9 23.2 1.0 N B:THR257 3.9 22.6 1.0 NH2 B:ARG59 4.0 20.0 1.0 CA B:GLY219 4.0 17.0 1.0 N B:THR221 4.2 19.9 1.0 C B:GLY219 4.2 17.5 1.0 O B:HOH1533 4.3 35.0 1.0 OG1 B:THR221 4.3 22.2 1.0 NH1 B:ARG59 4.3 19.9 1.0 CA B:GLY256 4.3 19.0 1.0 CA B:ILE220 4.5 18.2 1.0 C4A B:PLP413 4.5 23.6 1.0 CB B:THR257 4.6 21.6 1.0 C B:GLY256 4.6 21.3 1.0 C4 B:PLP413 4.6 24.4 1.0 CZ B:ARG59 4.7 18.3 1.0 C6 B:PLP413 4.8 23.9 1.0 CB B:ILE220 4.8 17.3 1.0 CB B:THR221 4.8 20.8 1.0 CA B:THR257 4.8 21.9 1.0 C B:ILE220 4.9 19.3 1.0 NE2 B:HIS56 4.9 13.7 1.0 NZ B:LYS159 5.0 23.2 1.0 O B:HOH1906 5.0 21.4 1.0

Phosphorus binding site 3 out of 3 in the Branched-Chain Amino Acid Aminotransferase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 3 of Branched-Chain Amino Acid Aminotransferase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ C:P413 b:16.9 occ:1.00 P C:PLP413 0.0 16.9 1.0 O1P C:PLP413 1.4 18.5 1.0 O2P C:PLP413 1.5 17.5 1.0 O3P C:PLP413 1.5 16.0 1.0 O4P C:PLP413 1.6 18.6 1.0 C5A C:PLP413 2.7 16.5 1.0 O C:HOH1538 3.4 17.9 1.0 N C:ILE220 3.4 19.2 1.0 N C:THR221 3.8 18.0 1.0 N C:THR257 3.8 21.1 1.0 OG1 C:THR221 3.8 11.6 1.0 NH2 C:ARG59 4.0 12.6 1.0 CA C:GLY219 4.0 18.1 1.0 OG1 C:THR257 4.1 24.0 1.0 C C:GLY219 4.1 18.7 1.0 C5 C:PLP413 4.2 17.0 1.0 CA C:ILE220 4.3 19.6 1.0 C4A C:PLP413 4.3 18.5 1.0 CA C:GLY256 4.3 18.0 1.0 CB C:THR221 4.4 14.5 1.0 C C:GLY256 4.5 20.2 1.0 NH1 C:ARG59 4.5 15.2 1.0 CB C:ILE220 4.5 18.4 1.0 C C:ILE220 4.5 18.9 1.0 CB C:THR257 4.5 22.8 1.0 CA C:THR257 4.7 22.9 1.0 C4 C:PLP413 4.7 17.2 1.0 CA C:THR221 4.7 15.0 1.0 CZ C:ARG59 4.7 14.2 1.0 NE2 C:HIS56 4.9 16.4 1.0 ND2 C:ASN198 4.9 24.6 1.0

K.Okada, K.Hirotsu, M.Sato, H.Hayashi, H.Kagamiyama. Three-Dimensional Structure of Escherichia Coli Branched-Chain Amino Acid Aminotransferase at 2.5 A Resolution. J.Biochem.(Tokyo) V. 121 637 1997.
ISSN: ISSN 0021-924X
PubMed: 9163511