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Sodium in PDB 4pyi: Human Apo Comt

Enzymatic activity of Human Apo Comt

All present enzymatic activity of Human Apo Comt:
2.1.1.6;

Protein crystallography data

The structure of Human Apo Comt, PDB code: 4pyi was solved by A.Ehler, J.Benz, D.Schlatter, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.77 / 1.35
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 31.596, 42.638, 43.663, 115.03, 95.35, 108.98
R / Rfree (%) 16.2 / 21.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Human Apo Comt (pdb code 4pyi). 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 Human Apo Comt, PDB code: 4pyi:

Sodium binding site 1 out of 1 in 4pyi

Go back to Sodium Binding Sites List in 4pyi
Sodium binding site 1 out of 1 in the Human Apo Comt


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Human Apo Comt within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na301

b:13.2
occ:1.00
O A:SER236 2.3 14.6 1.0
O A:PHE239 2.4 15.0 1.0
O A:VAL233 2.4 9.4 1.0
O A:HOH401 2.4 35.3 1.0
O A:ARG234 2.5 13.4 1.0
O A:HOH449 2.7 26.5 1.0
HA A:ARG234 3.1 9.6 1.0
C A:ARG234 3.2 9.8 1.0
HG A:CYS241 3.3 16.4 1.0
C A:SER236 3.4 12.5 1.0
HB2 A:PHE239 3.5 13.5 1.0
C A:PHE239 3.5 10.7 1.0
C A:VAL233 3.5 8.7 1.0
H A:PHE239 3.6 13.5 1.0
CA A:ARG234 3.6 8.0 1.0
H A:SER236 3.7 12.9 1.0
N A:SER236 3.7 10.7 1.0
HB3 A:SER236 4.0 18.5 1.0
N A:ARG234 4.0 8.2 1.0
CA A:SER236 4.1 12.9 1.0
N A:GLY235 4.1 8.8 1.0
C A:GLY235 4.1 9.7 1.0
HA A:GLU240 4.2 14.0 1.0
CA A:PHE239 4.2 11.5 1.0
CB A:PHE239 4.2 11.2 1.0
N A:PHE239 4.2 11.3 1.0
HA A:SER237 4.2 20.2 1.0
SG A:CYS241 4.3 13.6 1.0
N A:SER237 4.5 14.9 1.0
H A:CYS241 4.5 14.8 1.0
HB3 A:PHE239 4.5 13.5 1.0
N A:GLU240 4.6 9.8 1.0
CA A:GLY235 4.6 9.5 1.0
CB A:SER236 4.6 15.4 1.0
O A:GLY235 4.6 13.1 1.0
HA A:VAL233 4.7 10.9 1.0
H A:GLY235 4.7 10.5 1.0
CA A:SER237 4.8 16.9 1.0
HA2 A:GLY235 4.8 11.4 1.0
CA A:VAL233 4.8 9.1 1.0
HB2 A:CYS241 4.8 14.0 1.0
CA A:GLU240 4.8 11.7 1.0
H A:ARG234 4.9 9.9 1.0
N A:CYS241 4.9 12.4 1.0
HA A:SER236 5.0 15.5 1.0
CB A:ARG234 5.0 7.7 1.0

Reference:

A.Ehler, J.Benz, D.Schlatter, M.G.Rudolph. Mapping the Conformational Space Accessible to Catechol-O-Methyltransferase. Acta Crystallogr.,Sect.D V. 70 2163 2014.
ISSN: ISSN 0907-4449
PubMed: 25084335
DOI: 10.1107/S1399004714012917
Page generated: Mon Oct 7 17:51:57 2024

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