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Sodium in PDB 8r43: Crystal Structure of Paradendryphiella Salina PL7C Alginate Lyase Mutant H110N in Complex with Tri-Mannuronic Acid

Protein crystallography data

The structure of Crystal Structure of Paradendryphiella Salina PL7C Alginate Lyase Mutant H110N in Complex with Tri-Mannuronic Acid, PDB code: 8r43 was solved by C.Wilkens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.70 / 0.87
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.06, 38.62, 74.63, 90, 116.76, 90
R / Rfree (%) 12 / 14.1

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Paradendryphiella Salina PL7C Alginate Lyase Mutant H110N in Complex with Tri-Mannuronic Acid (pdb code 8r43). 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 Crystal Structure of Paradendryphiella Salina PL7C Alginate Lyase Mutant H110N in Complex with Tri-Mannuronic Acid, PDB code: 8r43:

Sodium binding site 1 out of 1 in 8r43

Go back to Sodium Binding Sites List in 8r43
Sodium binding site 1 out of 1 in the Crystal Structure of Paradendryphiella Salina PL7C Alginate Lyase Mutant H110N in Complex with Tri-Mannuronic Acid


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Paradendryphiella Salina PL7C Alginate Lyase Mutant H110N in Complex with Tri-Mannuronic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na301

b:8.7
occ:1.00
HH12 A:ARG232 2.4 9.6 1.0
HZ3 A:LYS234 2.5 9.6 0.7
HH22 A:ARG232 2.6 9.6 1.0
HB3 A:PRO109 2.9 9.6 0.1
HB3 A:PRO109 3.0 9.6 0.9
HE2 A:LYS234 3.1 9.6 1.0
NZ A:LYS234 3.2 9.5 1.0
O A:HOH792 3.2 12.2 1.0
O A:HOH789 3.2 10.9 1.0
HZ2 A:LYS234 3.2 9.6 1.0
NH1 A:ARG232 3.2 9.5 1.0
NH2 A:ARG232 3.3 9.3 1.0
HD3 A:LYS234 3.4 9.6 0.8
CE A:LYS234 3.6 9.0 1.0
CZ A:ARG232 3.8 8.7 1.0
CB A:PRO109 3.8 9.5 0.1
HG3 A:PRO109 3.8 9.6 0.1
CB A:PRO109 3.8 9.1 0.9
HH11 A:ARG232 3.9 9.6 1.0
HZ1 A:LYS234 3.9 9.6 1.0
O A:HOH626 3.9 19.2 1.0
HB2 A:PRO109 4.0 9.6 0.9
HB2 A:PRO109 4.0 9.6 0.1
CD A:LYS234 4.0 8.6 1.0
HH21 A:ARG232 4.0 9.6 1.0
HG3 A:PRO109 4.2 9.6 0.9
CG A:PRO109 4.3 9.5 0.1
HE3 A:LYS234 4.4 9.6 1.0
HG3 A:LYS234 4.5 9.6 1.0
CG A:PRO109 4.6 8.9 0.9
HG13 A:VAL107 4.7 9.6 1.0
O A:HOH729 4.7 39.0 1.0
HG12 A:VAL107 4.7 9.6 1.0
HE22 A:GLN61 4.7 9.6 0.5
HD2 A:LYS234 4.7 9.6 1.0
HD3 A:PRO109 4.8 9.6 0.1
HA A:PRO109 4.9 9.6 0.9
CG A:LYS234 4.9 8.2 1.0
HA A:PRO109 4.9 9.6 0.1
CA A:PRO109 5.0 8.3 0.9
CA A:PRO109 5.0 9.2 0.1

Reference:

C.Wilkens, C.Wilkens. N/A N/A.
Page generated: Wed Oct 9 13:19:20 2024

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