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Magnesium in PDB 7ujp: Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B

Enzymatic activity of Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B

All present enzymatic activity of Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B:
2.7.11.17;

Protein crystallography data

The structure of Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B, PDB code: 7ujp was solved by C.Ozden, J.C.Foster, M.M.Stratton, S.C.Garman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.56 / 2.56
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 73.143, 91.423, 91.922, 90, 90, 90
R / Rfree (%) 23.2 / 28.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B (pdb code 7ujp). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B, PDB code: 7ujp:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 7ujp

Go back to Magnesium Binding Sites List in 7ujp
Magnesium binding site 1 out of 3 in the Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:46.9
occ:1.00
O2A A:ADP301 1.9 80.7 1.0
OD1 A:ASN140 2.0 32.6 1.0
OD2 A:ASP156 2.6 36.0 1.0
CG A:ASN140 3.2 31.0 1.0
PA A:ADP301 3.4 74.8 1.0
O A:GLU139 3.5 31.0 1.0
CG A:ASP156 3.6 34.3 1.0
CB A:ASP156 3.9 32.1 1.0
ND2 A:ASN140 4.0 29.7 1.0
C A:GLU139 4.0 29.6 1.0
O3B A:ADP301 4.1 81.4 1.0
CA A:ASN140 4.2 29.3 1.0
C5' A:ADP301 4.2 60.7 1.0
O5' A:ADP301 4.2 69.4 1.0
O1A A:ADP301 4.3 73.1 1.0
O3A A:ADP301 4.3 74.2 1.0
CB A:ASN140 4.3 30.0 1.0
C3' A:ADP301 4.3 52.5 1.0
N A:ASN140 4.3 30.1 1.0
CB A:GLU139 4.5 29.2 1.0
C2' A:ADP301 4.6 49.8 1.0
MG C:MG1401 4.7 31.0 1.0
OD1 A:ASP156 4.8 34.5 1.0
C4' A:ADP301 4.9 55.7 1.0
OE1 A:GLU96 4.9 33.4 1.0
PB A:ADP301 4.9 80.5 1.0
CE A:LYS137 4.9 26.3 1.0
CA A:GLU139 5.0 29.5 1.0

Magnesium binding site 2 out of 3 in 7ujp

Go back to Magnesium Binding Sites List in 7ujp
Magnesium binding site 2 out of 3 in the Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg302

b:66.7
occ:1.00
OD2 B:ASP156 2.2 39.8 1.0
O2A B:ATP301 2.6 51.9 1.0
O B:GLU139 2.7 26.7 1.0
OD1 B:ASN140 2.9 27.1 1.0
O2B B:ATP301 3.1 53.5 1.0
CG B:ASP156 3.4 39.0 1.0
OE1 B:GLU96 3.6 31.1 1.0
C B:GLU139 3.6 26.3 1.0
C3' B:ATP301 3.6 44.4 1.0
C2' B:ATP301 3.8 42.1 1.0
C5' B:ATP301 3.8 49.1 1.0
PA B:ATP301 3.9 53.8 1.0
CG B:ASN140 4.0 25.6 1.0
CA B:ASN140 4.1 24.4 1.0
N B:ASN140 4.2 24.9 1.0
O3A B:ATP301 4.2 54.0 1.0
OD1 B:ASP156 4.2 41.1 1.0
PB B:ATP301 4.3 58.2 1.0
C4' B:ATP301 4.3 46.8 1.0
O2' B:ATP301 4.3 40.4 1.0
O5' B:ATP301 4.4 51.2 1.0
CB B:GLU139 4.4 25.9 1.0
CB B:ASP156 4.4 35.6 1.0
CD B:GLU96 4.6 27.5 1.0
CA B:GLU139 4.6 25.8 1.0
CB B:ASN140 4.7 24.6 1.0
O3' B:ATP301 4.8 44.6 1.0
O1G B:ATP301 4.9 59.8 1.0

Magnesium binding site 3 out of 3 in 7ujp

Go back to Magnesium Binding Sites List in 7ujp
Magnesium binding site 3 out of 3 in the Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1401

b:31.0
occ:1.00
OG C:SER1303 2.9 38.9 1.0
O3A A:ADP301 3.3 74.2 1.0
N C:SER1303 3.6 38.1 1.0
O2B A:ADP301 3.7 79.7 1.0
NZ A:LYS137 3.8 26.3 1.0
O2A A:ADP301 3.9 80.7 1.0
PA A:ADP301 4.0 74.8 1.0
CB C:SER1303 4.0 39.6 1.0
PB A:ADP301 4.1 80.5 1.0
CA C:HIS1302 4.2 39.0 1.0
O1A A:ADP301 4.3 73.1 1.0
C C:HIS1302 4.4 38.0 1.0
CA C:SER1303 4.4 39.7 1.0
O3B A:ADP301 4.6 81.4 1.0
ND1 C:HIS1302 4.6 45.0 1.0
O C:GLN1301 4.7 35.0 1.0
CE A:LYS137 4.7 26.3 1.0
MG A:MG302 4.7 46.9 1.0
OD2 A:ASP156 4.9 36.0 1.0
CB C:HIS1302 4.9 40.7 1.0

Reference:

C.Ozden, R.Sloutsky, T.Mitsugi, N.Santos, E.Agnello, C.Gaubitz, J.Foster, E.Lapinskas, E.A.Esposito, T.Saneyoshi, B.A.Kelch, S.C.Garman, Y.Hayashi, M.M.Stratton. Camkii Binds Both Substrates and Activators at the Active Site. Cell Rep V. 40 11064 2022.
ISSN: ESSN 2211-1247
PubMed: 35830796
DOI: 10.1016/J.CELREP.2022.111064
Page generated: Thu Oct 3 10:06:38 2024

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