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Atomistry » Potassium » PDB 5g17-5imu » 5hp4 » |
Potassium in PDB 5hp4: Crystal Structure Bacteriohage T5 D15 Flap Endonuclease (D155K) Pseudo-Enzyme-Product Complex with Dna and Metal IonsEnzymatic activity of Crystal Structure Bacteriohage T5 D15 Flap Endonuclease (D155K) Pseudo-Enzyme-Product Complex with Dna and Metal Ions
All present enzymatic activity of Crystal Structure Bacteriohage T5 D15 Flap Endonuclease (D155K) Pseudo-Enzyme-Product Complex with Dna and Metal Ions:
3.1.11.3; Protein crystallography data
The structure of Crystal Structure Bacteriohage T5 D15 Flap Endonuclease (D155K) Pseudo-Enzyme-Product Complex with Dna and Metal Ions, PDB code: 5hp4
was solved by
F.A.Almalki,
J.Zhang,
S.E.Sedelnikova,
J.B.Rafferty,
J.R.Sayers,
P.A.Artymiuk,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5hp4:
The structure of Crystal Structure Bacteriohage T5 D15 Flap Endonuclease (D155K) Pseudo-Enzyme-Product Complex with Dna and Metal Ions also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure Bacteriohage T5 D15 Flap Endonuclease (D155K) Pseudo-Enzyme-Product Complex with Dna and Metal Ions
(pdb code 5hp4). 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 Crystal Structure Bacteriohage T5 D15 Flap Endonuclease (D155K) Pseudo-Enzyme-Product Complex with Dna and Metal Ions, PDB code: 5hp4: Potassium binding site 1 out of 1 in 5hp4Go back to Potassium Binding Sites List in 5hp4
Potassium binding site 1 out
of 1 in the Crystal Structure Bacteriohage T5 D15 Flap Endonuclease (D155K) Pseudo-Enzyme-Product Complex with Dna and Metal Ions
Mono view Stereo pair view
Reference:
F.A.Almalki,
C.S.Flemming,
J.Zhang,
M.Feng,
S.E.Sedelnikova,
T.Ceska,
J.B.Rafferty,
J.R.Sayers,
P.J.Artymiuk.
Direct Observation of Dna Threading in Flap Endonuclease Complexes. Nat.Struct.Mol.Biol. V. 23 640 2016.
Page generated: Sun Dec 13 23:59:03 2020
ISSN: ESSN 1545-9985 PubMed: 27273516 DOI: 10.1038/NSMB.3241 |
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