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Sodium in PDB 4w82: Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase

Enzymatic activity of Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase

All present enzymatic activity of Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase:
1.3.1.39;

Protein crystallography data

The structure of Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase, PDB code: 4w82 was solved by K.H.Sippel, N.K.Vyas, B.Sankaran, F.A.Quiocho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.27 / 1.70
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 42.310, 59.040, 61.430, 94.96, 101.11, 95.09
R / Rfree (%) 18.7 / 21.7

Other elements in 4w82:

The structure of Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase (pdb code 4w82). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase, PDB code: 4w82:

Sodium binding site 1 out of 1 in 4w82

Go back to Sodium Binding Sites List in 4w82
Sodium binding site 1 out of 1 in the Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Enoyl-Acyl Carrier Protein-Reductase Domain From Human Fatty Acid Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na1902

b:25.2
occ:1.00
 OD2 B:ASP1575 2.5 17.5 1.0
O B:SER1570 2.8 18.1 1.0
ND2 B:ASN1572 2.9 13.5 1.0
N B:MET1601 3.0 16.2 1.0
O B:HOH2050 3.4 14.7 1.0
CG B:MET1601 3.5 20.1 1.0
N B:ASN1572 3.5 14.9 1.0
CG B:ASP1575 3.5 18.4 1.0
CA B:GLY1600 3.6 14.9 1.0
C B:SER1570 3.7 16.1 1.0
C B:GLY1600 3.7 17.5 1.0
CG B:ASN1572 3.8 16.3 1.0
CB B:ASN1572 3.8 15.0 1.0
OD1 B:ASP1575 3.8 18.2 1.0
N B:GLU1602 3.9 16.5 1.0
C B:LEU1571 3.9 17.8 1.0
CA B:MET1601 4.0 18.7 1.0
CA B:LEU1571 4.0 15.1 1.0
OG B:SER1570 4.0 24.7 1.0
CA B:ASN1572 4.3 14.7 1.0
CB B:MET1601 4.3 19.9 1.0
C B:MET1601 4.3 18.4 1.0
N B:LEU1571 4.3 15.2 1.0
CB B:GLU1602 4.3 19.1 1.0
N B:GLY1600 4.4 15.1 1.0
CA B:GLU1602 4.7 16.4 1.0
SD B:MET1601 4.8 30.8 1.0
O B:LEU1571 4.8 17.6 1.0
CA B:SER1570 4.8 17.1 1.0
CB B:ASP1575 4.8 16.4 1.0
O B:GLU1602 4.9 14.9 1.0
O B:GLY1600 4.9 17.1 1.0
OD1 B:ASN1572 5.0 14.5 1.0

Reference:

K.H.Sippel, N.K.Vyas, W.Zhang, B.Sankaran, F.A.Quiocho. Crystal Structure of the Human Fatty Acid Synthase Enoyl-Acyl Carrier Protein-Reductase Domain Complexed with Triclosan Reveals Allosteric Protein-Protein Interface Inhibition. J.Biol.Chem. 2014.
ISSN: ESSN 1083-351X
PubMed: 25301948
DOI: 10.1074/JBC.M114.608547
Page generated: Tue Dec 15 09:22:26 2020

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