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Sodium in PDB 4chi: (R)-Selective Amine Transaminase From Aspergillus Fumigatus at 1.27 A Resolution

Enzymatic activity of (R)-Selective Amine Transaminase From Aspergillus Fumigatus at 1.27 A Resolution

All present enzymatic activity of (R)-Selective Amine Transaminase From Aspergillus Fumigatus at 1.27 A Resolution:
2.6.1.18;

Protein crystallography data

The structure of (R)-Selective Amine Transaminase From Aspergillus Fumigatus at 1.27 A Resolution, PDB code: 4chi was solved by M.Thomsen, G.J.Palm, W.Hinrichs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.88 / 1.27
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 102.367, 120.935, 135.464, 90.00, 90.00, 90.00
R / Rfree (%) 10.329 / 12.697

Other elements in 4chi:

The structure of (R)-Selective Amine Transaminase From Aspergillus Fumigatus at 1.27 A Resolution also contains other interesting chemical elements:

Potassium (K) 6 atoms
Chlorine (Cl) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the (R)-Selective Amine Transaminase From Aspergillus Fumigatus at 1.27 A Resolution (pdb code 4chi). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the (R)-Selective Amine Transaminase From Aspergillus Fumigatus at 1.27 A Resolution, PDB code: 4chi:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 4chi

Go back to Sodium Binding Sites List in 4chi
Sodium binding site 1 out of 2 in the (R)-Selective Amine Transaminase From Aspergillus Fumigatus at 1.27 A Resolution


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of (R)-Selective Amine Transaminase From Aspergillus Fumigatus at 1.27 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na500

b:13.8
occ:0.50
O A:HOH1066 0.4 20.0 0.5
O3 A:PLP400 1.8 30.4 0.5
O3 A:PLP400 2.6 9.9 0.3
OH A:TYR58 2.6 11.4 1.0
O A:HOH1030 2.8 11.8 1.0
O A:HOH1534 2.8 17.6 0.2
NE1 A:TRP183 3.1 9.8 1.0
C3 A:PLP400 3.2 16.8 0.5
O A:ASN180 3.3 8.8 1.0
CZ A:TYR58 3.5 10.2 1.0
C3 A:PLP400 3.5 7.8 0.3
CE1 A:TYR58 3.6 10.5 1.0
NZ A:LYS179 3.6 20.6 0.5
C2A A:PLP400 3.7 8.4 0.3
C2A A:PLP400 3.7 20.7 0.5
CE2 A:TRP183 3.7 9.7 1.0
CZ2 A:TRP183 3.7 12.2 1.0
CG A:LYS179 3.9 12.8 0.5
CG A:LYS179 3.9 9.7 0.5
C2 A:PLP400 4.0 17.0 0.5
O A:HOH1028 4.0 12.9 1.0
CE A:LYS179 4.0 11.1 0.5
C2 A:PLP400 4.1 7.7 0.3
CD1 A:TRP183 4.2 9.5 1.0
C4 A:PLP400 4.2 17.1 0.5
N A:ASN180 4.3 8.2 1.0
CE A:LYS179 4.3 16.4 0.5
C A:ASN180 4.4 7.9 1.0
C4A A:PLP400 4.4 16.4 0.5
CD A:LYS179 4.6 10.1 0.5
C4 A:PLP400 4.7 9.3 0.3
CD A:LYS179 4.7 14.7 0.5
O A:HOH1065 4.7 17.6 1.0
CE2 A:TYR58 4.8 10.4 1.0
CD1 A:TYR58 4.9 9.5 1.0
O A:HOH1528 5.0 13.1 0.2
NZ A:LYS179 5.0 13.0 0.5

Sodium binding site 2 out of 2 in 4chi

Go back to Sodium Binding Sites List in 4chi
Sodium binding site 2 out of 2 in the (R)-Selective Amine Transaminase From Aspergillus Fumigatus at 1.27 A Resolution


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of (R)-Selective Amine Transaminase From Aspergillus Fumigatus at 1.27 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na500

b:16.1
occ:0.50
O B:HOH1468 0.5 15.1 0.5
O3 B:PLP400 1.8 23.4 0.4
O3 B:PLP400 2.5 10.8 0.4
OH B:TYR58 2.7 11.6 1.0
O B:HOH1047 2.8 12.9 1.0
C3 B:PLP400 3.1 16.5 0.4
NE1 B:TRP183 3.1 10.4 1.0
C3 B:PLP400 3.4 10.7 0.4
O B:ASN180 3.4 9.3 1.0
CZ B:TYR58 3.6 10.0 1.0
NZ B:LYS179 3.6 20.1 0.4
C2A B:PLP400 3.6 11.6 0.4
CZ2 B:TRP183 3.7 12.3 1.0
CE1 B:TYR58 3.7 10.2 1.0
CE2 B:TRP183 3.7 9.6 1.0
C2A B:PLP400 3.7 18.6 0.4
C2 B:PLP400 3.9 9.9 0.4
CG B:LYS179 3.9 12.9 0.6
CE B:LYS179 3.9 14.8 0.6
C2 B:PLP400 3.9 14.8 0.4
CG B:LYS179 4.0 11.3 0.4
O B:HOH1048 4.1 13.4 1.0
C4 B:PLP400 4.2 15.2 0.4
CD1 B:TRP183 4.3 9.5 1.0
C4A B:PLP400 4.3 12.9 0.4
CE B:LYS179 4.3 17.8 0.4
N B:ASN180 4.4 9.2 1.0
CD B:LYS179 4.5 13.8 0.6
C B:ASN180 4.5 8.5 1.0
C4 B:PLP400 4.6 13.1 0.4
O A:HOH1076 4.7 18.0 1.0
CD B:LYS179 4.8 13.7 0.4
CE2 B:TYR58 4.8 10.8 1.0
O B:HOH1448 4.9 15.1 0.2
C4A B:PLP400 4.9 12.9 0.4
CH2 B:TRP183 5.0 13.8 1.0
NZ B:LYS179 5.0 16.7 0.6
CD1 B:TYR58 5.0 9.8 1.0

Reference:

M.Thomsen, L.Skalden, G.J.Palm, M.Hohne, U.T.Bornscheuer, W.Hinrichs. Crystallographic Characterization of the (R)-Selective Amine Transaminase From Aspergillus Fumigatus. Acta Crystallogr.,Sect.D V. 70 1086 2014.
ISSN: ISSN 0907-4449
PubMed: 24699652
DOI: 10.1107/S1399004714001084
Page generated: Tue Dec 15 06:35:47 2020

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