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Sodium in PDB 1qtk: Crystal Structure of Hew Lysozyme Under Pressure of Krypton (55 Bar)

Enzymatic activity of Crystal Structure of Hew Lysozyme Under Pressure of Krypton (55 Bar)

All present enzymatic activity of Crystal Structure of Hew Lysozyme Under Pressure of Krypton (55 Bar):
3.2.1.17;

Protein crystallography data

The structure of Crystal Structure of Hew Lysozyme Under Pressure of Krypton (55 Bar), PDB code: 1qtk was solved by T.Prange, M.Schiltz, L.Pernot, N.Colloc'h, S.Longhi, W.Bourguet, R.Fourme, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 9.90 / 2.03
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.530, 78.530, 37.740, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 21.6

Other elements in 1qtk:

The structure of Crystal Structure of Hew Lysozyme Under Pressure of Krypton (55 Bar) also contains other interesting chemical elements:

Krypton (Kr) 1 atom
Chlorine (Cl) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Hew Lysozyme Under Pressure of Krypton (55 Bar) (pdb code 1qtk). 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 Hew Lysozyme Under Pressure of Krypton (55 Bar), PDB code: 1qtk:

Sodium binding site 1 out of 1 in 1qtk

Go back to Sodium Binding Sites List in 1qtk
Sodium binding site 1 out of 1 in the Crystal Structure of Hew Lysozyme Under Pressure of Krypton (55 Bar)


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 Hew Lysozyme Under Pressure of Krypton (55 Bar) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na140

b:30.8
occ:1.00
OG A:SER72 2.2 33.4 1.0
O A:SER60 2.3 17.7 1.0
O A:HOH202 2.5 17.5 1.0
O A:CYS64 2.6 13.5 1.0
O A:HOH222 2.6 26.2 1.0
O A:ARG73 2.7 35.5 1.0
CB A:SER72 2.7 28.5 1.0
C A:SER60 3.4 14.8 1.0
C A:ARG73 3.6 24.5 1.0
C A:CYS64 3.6 16.5 1.0
C A:SER72 3.7 33.9 1.0
N A:ARG73 3.8 26.1 1.0
CA A:SER72 3.8 30.5 1.0
CA A:ASN65 4.0 11.7 1.0
O A:ARG61 4.0 22.3 1.0
O A:SER72 4.2 27.7 1.0
C A:ARG61 4.2 18.4 1.0
CA A:SER60 4.2 15.9 1.0
N A:ASN65 4.3 10.4 1.0
CA A:ARG73 4.3 25.4 1.0
N A:CYS64 4.4 14.4 1.0
N A:ASN74 4.5 19.1 1.0
N A:ARG61 4.5 17.2 1.0
CL A:CL162 4.5 49.8 1.0
CA A:ARG61 4.5 27.8 1.0
CB A:SER60 4.6 14.8 1.0
CB A:THR69 4.6 17.7 1.0
ND2 A:ASN65 4.6 26.2 1.0
CA A:CYS64 4.7 13.5 1.0
CA A:ASN74 4.7 18.9 1.0
O A:THR69 4.7 29.3 1.0
N A:TRP62 4.8 18.2 1.0
N A:ASP66 4.8 9.4 1.0
N A:SER72 4.8 22.4 1.0
CB A:ASN65 4.9 20.2 1.0
CB A:ASN74 4.9 17.9 1.0
C A:ASN65 5.0 13.0 1.0

Reference:

T.Prange, M.Schiltz, L.Pernot, N.Colloc'h, S.Longhi, W.Bourguet, R.Fourme. Exploring Hydrophobic Sites in Proteins with Xenon or Krypton. Proteins V. 30 61 1998.
ISSN: ISSN 0887-3585
PubMed: 9443341
DOI: 10.1002/(SICI)1097-0134(19980101)30:1<61::AID-PROT6>3.3.CO;2-O
Page generated: Tue Dec 15 05:34:34 2020

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