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Potassium in PDB 4wub: N-Terminal 43 kDa Fragment of the E. Coli Dna Gyrase B Subunit Grown From 100 Mm Kcl Condition

Enzymatic activity of N-Terminal 43 kDa Fragment of the E. Coli Dna Gyrase B Subunit Grown From 100 Mm Kcl Condition

All present enzymatic activity of N-Terminal 43 kDa Fragment of the E. Coli Dna Gyrase B Subunit Grown From 100 Mm Kcl Condition:
5.99.1.3;

Protein crystallography data

The structure of N-Terminal 43 kDa Fragment of the E. Coli Dna Gyrase B Subunit Grown From 100 Mm Kcl Condition, PDB code: 4wub was solved by S.J.Hearnshaw, T.T.Chung, C.E.M.Stevenson, A.Maxwell, D.M.Lawson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.74 / 1.75
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 87.880, 140.900, 79.560, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 20.4

Other elements in 4wub:

The structure of N-Terminal 43 kDa Fragment of the E. Coli Dna Gyrase B Subunit Grown From 100 Mm Kcl Condition also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Chlorine (Cl) 1 atom
Sodium (Na) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the N-Terminal 43 kDa Fragment of the E. Coli Dna Gyrase B Subunit Grown From 100 Mm Kcl Condition (pdb code 4wub). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the N-Terminal 43 kDa Fragment of the E. Coli Dna Gyrase B Subunit Grown From 100 Mm Kcl Condition, PDB code: 4wub:

Potassium binding site 1 out of 1 in 4wub

Go back to Potassium Binding Sites List in 4wub
Potassium binding site 1 out of 1 in the N-Terminal 43 kDa Fragment of the E. Coli Dna Gyrase B Subunit Grown From 100 Mm Kcl Condition


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of N-Terminal 43 kDa Fragment of the E. Coli Dna Gyrase B Subunit Grown From 100 Mm Kcl Condition within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K403

b:27.1
occ:1.00
O A:ILE94 2.7 26.3 1.0
O A:GLY117 2.7 23.4 1.0
O2A A:ANP401 2.8 24.1 1.0
OG A:SER121 2.8 26.9 1.0
O A:ALA100 2.9 26.9 1.0
O A:VAL97 3.0 28.3 1.0
C A:GLY117 3.5 24.5 1.0
CB A:SER121 3.6 28.0 1.0
C A:ILE94 3.7 28.4 1.0
C A:ALA100 4.0 26.4 1.0
N A:VAL118 4.1 23.2 1.0
C5' A:ANP401 4.1 26.6 1.0
PA A:ANP401 4.1 25.9 1.0
C A:VAL97 4.1 27.8 1.0
CA A:ILE94 4.1 29.8 1.0
N A:ALA100 4.2 26.2 1.0
CA A:VAL118 4.3 25.5 1.0
CA A:GLY117 4.3 23.6 1.0
N A:SER121 4.4 26.0 1.0
CB A:ALA100 4.4 26.9 1.0
CA A:ALA100 4.4 26.4 1.0
C A:VAL118 4.5 24.9 1.0
CA A:SER121 4.6 27.6 1.0
O3A A:ANP401 4.6 25.8 1.0
O A:VAL118 4.6 22.8 1.0
O5' A:ANP401 4.6 25.7 1.0
O A:VAL93 4.7 30.0 1.0
CA A:LEU98 4.8 27.2 1.0
N A:HIS99 4.8 25.1 1.0
N A:LEU98 4.9 27.8 1.0
CG2 A:ILE94 4.9 32.2 1.0
N A:MET95 4.9 29.9 1.0
N A:VAL97 4.9 29.9 1.0

Reference:

S.J.Hearnshaw, T.T.Chung, C.E.M.Stevenson, A.Maxwell, D.M.Lawson. The Role of Monovalent Cations in the Atpase Reaction of Dna Gyrase Acta Crystallogr.,Sect.D V. 71 996 2015.
ISSN: ESSN 1399-0047
DOI: 10.1107/S1399004715002916
Page generated: Mon Aug 12 12:21:50 2024

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