Manganese in PDB 1jst: Phosphorylated Cyclin-Dependent Kinase-2 Bound to Cyclin A

The structure of Phosphorylated Cyclin-Dependent Kinase-2 Bound to Cyclin A, PDB code: 1jst was solved by A.A.Russo, P.D.Jeffrey, N.P.Pavletich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	139.600, 149.100, 74.200, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Manganese atom in the Phosphorylated Cyclin-Dependent Kinase-2 Bound to Cyclin A (pdb code 1jst). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Phosphorylated Cyclin-Dependent Kinase-2 Bound to Cyclin A, PDB code: 1jst:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Phosphorylated Cyclin-Dependent Kinase-2 Bound to Cyclin A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Phosphorylated Cyclin-Dependent Kinase-2 Bound to Cyclin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn299 b:48.5 occ:1.00 OD1 A:ASN132 2.3 15.0 1.0 O2A A:ATP300 2.5 90.0 1.0 OD2 A:ASP145 2.9 36.8 1.0 O5' A:ATP300 3.4 90.0 1.0 CG A:ASN132 3.5 12.7 1.0 CG A:ASP145 3.6 31.9 1.0 CB A:ASP145 3.7 26.5 1.0 PA A:ATP300 3.7 90.0 1.0 O1G A:ATP300 4.2 89.9 1.0 C5' A:ATP300 4.2 89.3 1.0 ND2 A:ASN132 4.2 12.5 1.0 O1B A:ATP300 4.3 90.0 1.0 CB A:ASN132 4.6 10.2 1.0 CA A:ASN132 4.7 15.7 1.0 O3A A:ATP300 4.7 90.0 1.0 OD1 A:ASP145 4.8 29.9 1.0 O1A A:ATP300 4.8 89.5 1.0 N A:ASN132 4.8 21.9 1.0 O A:GLN131 4.9 28.3 1.0 C3' A:ATP300 4.9 88.0 1.0 O3' A:ATP300 5.0 88.3 1.0 C A:GLN131 5.0 24.8 1.0

Manganese binding site 2 out of 2 in the Phosphorylated Cyclin-Dependent Kinase-2 Bound to Cyclin A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Phosphorylated Cyclin-Dependent Kinase-2 Bound to Cyclin A within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn299 b:24.4 occ:1.00 OD1 C:ASN132 2.2 21.1 1.0 O2G C:ATP300 2.4 90.0 1.0 O5' C:ATP300 2.5 76.3 1.0 C5' C:ATP300 2.9 75.5 1.0 OD2 C:ASP145 3.1 43.5 1.0 CG C:ASN132 3.5 20.4 1.0 O3A C:ATP300 3.6 80.9 1.0 PA C:ATP300 3.7 77.8 1.0 CG C:ASP145 3.9 41.2 1.0 PG C:ATP300 4.0 90.0 1.0 O2A C:ATP300 4.1 78.6 1.0 O3' C:ATP300 4.1 73.3 1.0 O1B C:ATP300 4.2 84.2 1.0 C4' C:ATP300 4.2 72.2 1.0 ND2 C:ASN132 4.2 20.6 1.0 CB C:ASP145 4.3 36.4 1.0 C3' C:ATP300 4.4 72.8 1.0 O C:GLN131 4.5 30.3 1.0 PB C:ATP300 4.6 84.5 1.0 CG C:GLN131 4.6 40.2 1.0 CB C:ASN132 4.6 21.4 1.0 O1G C:ATP300 4.6 90.0 1.0 CA C:ASN132 4.6 22.9 1.0 O3B C:ATP300 4.7 87.8 1.0 C C:GLN131 4.8 28.5 1.0 O1A C:ATP300 4.9 77.8 1.0 OD1 C:ASP145 4.9 42.7 1.0 N C:ASN132 4.9 26.1 1.0 O3G C:ATP300 4.9 90.0 1.0 NE2 C:GLN131 5.0 49.8 1.0

A.A.Russo, P.D.Jeffrey, N.P.Pavletich. Structural Basis of Cyclin-Dependent Kinase Activation By Phosphorylation. Nat.Struct.Biol. V. 3 696 1996.
ISSN: ISSN 1072-8368
PubMed: 8756328
DOI: 10.1038/NSB0896-696