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Magnesium in PDB 1fq1: Crystal Structure of Kinase Associated Phosphatase (Kap) in Complex with Phospho-CDK2

Enzymatic activity of Crystal Structure of Kinase Associated Phosphatase (Kap) in Complex with Phospho-CDK2

All present enzymatic activity of Crystal Structure of Kinase Associated Phosphatase (Kap) in Complex with Phospho-CDK2:
2.7.11.22; 3.1.3.48;

Protein crystallography data

The structure of Crystal Structure of Kinase Associated Phosphatase (Kap) in Complex with Phospho-CDK2, PDB code: 1fq1 was solved by H.Song, N.Hanlon, N.R.Brown, M.E.M.Noble, L.N.Johnson, D.Barford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 3.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 134.450, 134.450, 65.800, 90.00, 90.00, 120.00
R / Rfree (%) 23.5 / 31.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Kinase Associated Phosphatase (Kap) in Complex with Phospho-CDK2 (pdb code 1fq1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Kinase Associated Phosphatase (Kap) in Complex with Phospho-CDK2, PDB code: 1fq1:

Magnesium binding site 1 out of 1 in 1fq1

Go back to Magnesium Binding Sites List in 1fq1
Magnesium binding site 1 out of 1 in the Crystal Structure of Kinase Associated Phosphatase (Kap) in Complex with Phospho-CDK2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Kinase Associated Phosphatase (Kap) in Complex with Phospho-CDK2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg383

b:65.7
occ:1.00
O1G B:ATP381 2.5 0.8 1.0
O2A B:ATP381 2.6 0.9 1.0
ND2 B:ASN132 2.6 90.0 1.0
O2G B:ATP381 2.6 0.9 1.0
CG B:ASN132 2.7 90.8 1.0
OD1 B:ASN132 2.7 92.0 1.0
PG B:ATP381 2.8 0.6 1.0
O3B B:ATP381 3.0 0.5 1.0
CB B:ASP145 3.2 79.3 1.0
PA B:ATP381 3.4 0.9 1.0
C5' B:ATP381 3.4 0.2 1.0
O3A B:ATP381 3.5 0.1 1.0
CB B:ASN132 3.7 90.0 1.0
CG B:ASP145 3.7 80.0 1.0
O B:GLN131 3.7 88.8 1.0
CA B:ASN132 3.8 88.5 1.0
OD2 B:ASP145 3.8 82.7 1.0
O5' B:ATP381 3.8 0.1 1.0
PB B:ATP381 4.0 0.4 1.0
C B:GLN131 4.2 87.8 1.0
N B:ASN132 4.3 88.7 1.0
O3G B:ATP381 4.3 0.9 1.0
OD1 B:ASP145 4.5 77.9 1.0
CA B:ASP145 4.6 80.9 1.0
C4' B:ATP381 4.7 0.8 1.0
N B:ASP145 4.8 81.5 1.0
O1A B:ATP381 4.8 0.7 1.0
O2B B:ATP381 4.9 0.4 1.0
OE1 B:GLN131 4.9 90.2 1.0
O1B B:ATP381 5.0 0.9 1.0

Reference:

H.Song, N.Hanlon, N.R.Brown, M.E.Noble, L.N.Johnson, D.Barford. Phosphoprotein-Protein Interactions Revealed By the Crystal Structure of Kinase-Associated Phosphatase in Complex with PHOSPHOCDK2. Mol.Cell V. 7 615 2001.
ISSN: ISSN 1097-2765
PubMed: 11463386
DOI: 10.1016/S1097-2765(01)00208-8
Page generated: Mon Dec 14 05:56:17 2020

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