Phosphorus in PDB 1ad4: Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus

Enzymatic activity of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus

All present enzymatic activity of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus:
2.5.1.15;

Protein crystallography data

The structure of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus, PDB code: 1ad4 was solved by C.Oefner, D.Kostrewa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 13.00 / 2.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 65.748, 42.142, 99.040, 90.00, 106.06, 90.00
R / Rfree (%) 17.6 / n/a

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus (pdb code 1ad4). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus, PDB code: 1ad4:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in 1ad4

Go back to Phosphorus Binding Sites List in 1ad4
Phosphorus binding site 1 out of 2 in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P271

b:15.1
occ:1.00
P1 A:HH2271 0.0 15.1 1.0
O1P A:HH2271 1.5 16.1 1.0
O2P A:HH2271 1.5 14.8 1.0
O3P A:HH2271 1.6 14.1 1.0
O4 A:HH2271 1.6 11.7 1.0
C11 A:HH2271 2.7 19.4 1.0
P2 A:HH2271 3.0 18.1 1.0
O6P A:HH2271 3.2 16.8 1.0
O4P A:HH2271 3.6 11.1 1.0
O A:HOH362 3.6 29.3 1.0
O A:HOH336 3.7 21.9 1.0
C2 A:HH2271 3.9 12.5 1.0
O5P A:HH2271 4.0 1.1 1.0
NE A:ARG52 4.2 34.9 1.0
MN A:MN269 4.2 37.7 1.0
C3 A:HH2271 4.3 14.6 1.0
CD A:ARG52 4.9 28.5 1.0
NH2 A:ARG52 4.9 33.7 1.0
OG A:SER50 4.9 33.3 1.0
CZ A:ARG52 5.0 33.5 1.0

Phosphorus binding site 2 out of 2 in 1ad4

Go back to Phosphorus Binding Sites List in 1ad4
Phosphorus binding site 2 out of 2 in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P271

b:18.1
occ:1.00
P2 A:HH2271 0.0 18.1 1.0
O4P A:HH2271 1.5 11.1 1.0
O6P A:HH2271 1.5 16.8 1.0
O5P A:HH2271 1.5 1.1 1.0
O3P A:HH2271 1.6 14.1 1.0
P1 A:HH2271 3.0 15.1 1.0
O4 A:HH2271 3.3 11.7 1.0
MN A:MN269 3.5 37.7 1.0
O2P A:HH2271 3.5 14.8 1.0
C11 A:HH2271 3.7 19.4 1.0
NH1 A:ARG239 4.1 10.7 1.0
NE2 A:HIS241 4.1 11.0 1.0
NH2 A:ARG239 4.1 9.9 1.0
O1P A:HH2271 4.1 16.1 1.0
O A:HOH336 4.1 21.9 1.0
O A:HOH325 4.2 12.0 1.0
C2 A:HH2271 4.2 12.5 1.0
OD1 A:ASN11 4.2 34.0 1.0
ND2 A:ASN11 4.3 26.4 1.0
CE1 A:HIS241 4.3 9.4 1.0
C3 A:HH2271 4.4 14.6 1.0
O A:HOH362 4.4 29.3 1.0
CZ A:ARG239 4.6 2.0 1.0
CG2 A:ILE9 4.6 6.3 1.0
CD1 A:ILE9 4.7 2.0 1.0
CG A:ASN11 4.7 28.4 1.0

Reference:

I.C.Hampele, A.D'arcy, G.E.Dale, D.Kostrewa, J.Nielsen, C.Oefner, M.G.Page, H.J.Schonfeld, D.Stuber, R.L.Then. Structure and Function of the Dihydropteroate Synthase From Staphylococcus Aureus. J.Mol.Biol. V. 268 21 1997.
ISSN: ISSN 0022-2836
PubMed: 9149138
DOI: 10.1006/JMBI.1997.0944
Page generated: Fri Sep 25 12:45:19 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