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Atomistry » Manganese » PDB 4k3v-4lt5 » 4lil | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 4k3v-4lt5 » 4lil » |
Manganese in PDB 4lil: Crystal Structure of the Catalytic Subunit of Human Primase Bound to Utp and MnProtein crystallography data
The structure of Crystal Structure of the Catalytic Subunit of Human Primase Bound to Utp and Mn, PDB code: 4lil
was solved by
S.Vaithiyalingam,
B.F.Eichman,
W.J.Chazin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4lil:
The structure of Crystal Structure of the Catalytic Subunit of Human Primase Bound to Utp and Mn also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of the Catalytic Subunit of Human Primase Bound to Utp and Mn
(pdb code 4lil). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of the Catalytic Subunit of Human Primase Bound to Utp and Mn, PDB code: 4lil: Jump to Manganese binding site number: 1; 2; Manganese binding site 1 out of 2 in 4lilGo back to![]() ![]()
Manganese binding site 1 out
of 2 in the Crystal Structure of the Catalytic Subunit of Human Primase Bound to Utp and Mn
![]() Mono view ![]() Stereo pair view
Manganese binding site 2 out of 2 in 4lilGo back to![]() ![]()
Manganese binding site 2 out
of 2 in the Crystal Structure of the Catalytic Subunit of Human Primase Bound to Utp and Mn
![]() Mono view ![]() Stereo pair view
Reference:
S.Vaithiyalingam,
D.R.Arnett,
A.Aggarwal,
B.F.Eichman,
E.Fanning,
W.J.Chazin.
Insights Into Eukaryotic Primer Synthesis From Structures of the P48 Subunit of Human Dna Primase. J.Mol.Biol. V. 426 558 2014.
Page generated: Sat Oct 5 20:06:42 2024
ISSN: ISSN 0022-2836 PubMed: 24239947 DOI: 10.1016/J.JMB.2013.11.007 |
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