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Manganese in PDB 1o6k: Structure of Activated Form of Pkb Kinase Domain S474D with GSK3 Peptide and Amp-Pnp

Enzymatic activity of Structure of Activated Form of Pkb Kinase Domain S474D with GSK3 Peptide and Amp-Pnp

All present enzymatic activity of Structure of Activated Form of Pkb Kinase Domain S474D with GSK3 Peptide and Amp-Pnp:
2.7.1.37;

Protein crystallography data

The structure of Structure of Activated Form of Pkb Kinase Domain S474D with GSK3 Peptide and Amp-Pnp, PDB code: 1o6k was solved by J.Yang, P.Cron, V.M.Good, V.Thompson, B.A.Hemmings, D.Barford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.89 / 1.7
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.906, 60.998, 129.410, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 23.4

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of Activated Form of Pkb Kinase Domain S474D with GSK3 Peptide and Amp-Pnp (pdb code 1o6k). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Activated Form of Pkb Kinase Domain S474D with GSK3 Peptide and Amp-Pnp, PDB code: 1o6k:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1o6k

Go back to Manganese Binding Sites List in 1o6k
Manganese binding site 1 out of 2 in the Structure of Activated Form of Pkb Kinase Domain S474D with GSK3 Peptide and Amp-Pnp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Activated Form of Pkb Kinase Domain S474D with GSK3 Peptide and Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1481

b:9.8
occ:1.00
O2A A:ANP1480 2.0 8.2 1.0
O2G A:ANP1480 2.1 8.4 1.0
OD1 A:ASN280 2.2 8.4 1.0
O A:HOH2265 2.2 8.1 1.0
OD2 A:ASP293 2.3 10.4 1.0
N3B A:ANP1480 2.8 10.8 1.0
PG A:ANP1480 3.1 9.8 1.0
CG A:ASN280 3.2 9.2 1.0
CG A:ASP293 3.2 11.1 1.0
PA A:ANP1480 3.4 10.1 1.0
ND2 A:ASN280 3.5 7.5 1.0
CB A:ASP293 3.6 9.8 1.0
PB A:ANP1480 3.8 11.6 1.0
CE A:LYS277 3.9 10.5 1.0
O1G A:ANP1480 3.9 10.1 1.0
O2B A:ANP1480 3.9 12.6 1.0
O3A A:ANP1480 3.9 11.5 1.0
MN A:MN1482 4.0 11.5 1.0
O3G A:ANP1480 4.2 10.9 1.0
OD1 A:ASP293 4.2 10.6 1.0
NZ A:LYS277 4.3 13.3 1.0
O1A A:ANP1480 4.4 9.4 1.0
O3' A:ANP1480 4.4 10.9 1.0
O C:HOH2005 4.4 31.4 1.0
O5' A:ANP1480 4.5 8.5 1.0
CB A:ASN280 4.5 6.4 1.0
C5' A:ANP1480 4.6 9.9 1.0
OD2 A:ASP275 4.6 8.8 1.0
C3' A:ANP1480 4.8 10.8 1.0
CA A:ASN280 4.8 7.7 1.0
O A:GLU279 4.9 8.9 1.0
O A:HOH2266 5.0 15.4 1.0
N A:ASN280 5.0 6.7 1.0
C A:GLU279 5.0 8.7 1.0

Manganese binding site 2 out of 2 in 1o6k

Go back to Manganese Binding Sites List in 1o6k
Manganese binding site 2 out of 2 in the Structure of Activated Form of Pkb Kinase Domain S474D with GSK3 Peptide and Amp-Pnp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Activated Form of Pkb Kinase Domain S474D with GSK3 Peptide and Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1482

b:11.5
occ:1.00
O1G A:ANP1480 2.2 10.1 1.0
O2B A:ANP1480 2.2 12.6 1.0
O A:HOH2267 2.2 13.3 1.0
O A:HOH2266 2.3 15.4 1.0
OD1 A:ASP293 2.3 10.6 1.0
OD2 A:ASP293 2.3 10.4 1.0
CG A:ASP293 2.6 11.1 1.0
PG A:ANP1480 3.3 9.8 1.0
PB A:ANP1480 3.4 11.6 1.0
N3B A:ANP1480 3.5 10.8 1.0
O2G A:ANP1480 3.7 8.4 1.0
OG C:SER9 4.0 14.8 1.0
MN A:MN1481 4.0 9.8 1.0
OD2 A:ASP275 4.1 8.8 1.0
O A:HOH2032 4.1 20.1 1.0
CB A:ASP293 4.2 9.8 1.0
O1B A:ANP1480 4.3 13.5 1.0
NZ A:LYS181 4.3 14.0 1.0
CA A:GLY295 4.4 10.4 1.0
O3A A:ANP1480 4.5 11.5 1.0
O2A A:ANP1480 4.5 8.2 1.0
O3G A:ANP1480 4.5 10.9 1.0
N A:GLY295 4.6 10.2 1.0
O A:HOH2111 4.7 30.1 1.0
CB C:SER9 4.7 14.6 1.0
PA A:ANP1480 4.8 10.1 1.0
O A:ASP293 5.0 11.2 1.0
CA A:ASP293 5.0 10.4 1.0
O1A A:ANP1480 5.0 9.4 1.0
C A:GLY295 5.0 12.1 1.0

Reference:

J.Yang, P.Cron, V.M.Good, V.Thompson, B.A.Hemmings, D.Barford. Crystal Structure of An Activated Akt/Protein Kinase B Ternary Complex with Gsk-3 Peptide and Amp-Pnp Nat.Struct.Biol. V. 9 940 2002.
ISSN: ISSN 1072-8368
PubMed: 12434148
DOI: 10.1038/NSB870
Page generated: Sat Oct 5 11:53:43 2024

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