Magnesium in PDB 1zyd: Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp.
Enzymatic activity of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp.
All present enzymatic activity of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp.:
2.7.1.37;
Protein crystallography data
The structure of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp., PDB code: 1zyd
was solved by
A.K.Padyana,
H.Qiu,
A.Roll-Mecak,
A.G.Hinnebusch,
S.K.Burley,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.59 /
2.75
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
82.110,
175.210,
47.570,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp.
(pdb code 1zyd). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp., PDB code: 1zyd:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 1zyd
Go back to
Magnesium Binding Sites List in 1zyd
Magnesium binding site 1 out
of 4 in the Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp.
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 EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg305
b:27.7
occ:1.00
|
O1A
|
A:ATP303
|
2.1
|
47.6
|
1.0
|
OD2
|
A:ASP853
|
2.5
|
34.7
|
1.0
|
OD1
|
A:ASP853
|
2.7
|
37.3
|
1.0
|
O2G
|
A:ATP303
|
2.8
|
52.0
|
1.0
|
O3G
|
A:ATP303
|
2.9
|
60.1
|
1.0
|
CG
|
A:ASP853
|
2.9
|
40.4
|
1.0
|
O3B
|
A:ATP303
|
3.0
|
54.9
|
1.0
|
PG
|
A:ATP303
|
3.0
|
49.3
|
1.0
|
PA
|
A:ATP303
|
3.4
|
46.2
|
1.0
|
OD1
|
A:ASP835
|
3.9
|
45.2
|
1.0
|
O
|
A:ASP853
|
4.1
|
32.7
|
1.0
|
O3A
|
A:ATP303
|
4.1
|
46.6
|
1.0
|
O2A
|
A:ATP303
|
4.1
|
45.0
|
1.0
|
MG
|
A:MG306
|
4.1
|
26.6
|
1.0
|
PB
|
A:ATP303
|
4.3
|
48.5
|
1.0
|
CB
|
A:ASP853
|
4.3
|
31.5
|
1.0
|
NZ
|
A:LYS628
|
4.5
|
40.1
|
1.0
|
O5'
|
A:ATP303
|
4.5
|
51.0
|
1.0
|
O1G
|
A:ATP303
|
4.5
|
52.5
|
1.0
|
OD1
|
A:ASN840
|
4.8
|
37.4
|
1.0
|
C
|
A:ASP853
|
4.8
|
32.0
|
1.0
|
ND2
|
A:ASN840
|
4.9
|
38.6
|
1.0
|
O
|
A:HOH64
|
4.9
|
35.8
|
1.0
|
O1B
|
A:ATP303
|
4.9
|
63.2
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 1zyd
Go back to
Magnesium Binding Sites List in 1zyd
Magnesium binding site 2 out
of 4 in the Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg306
b:26.6
occ:1.00
|
OD1
|
A:ASN840
|
2.2
|
37.4
|
1.0
|
O3B
|
A:ATP303
|
2.4
|
54.9
|
1.0
|
OD2
|
A:ASP853
|
2.5
|
34.7
|
1.0
|
CG
|
A:ASN840
|
3.3
|
33.4
|
1.0
|
PB
|
A:ATP303
|
3.3
|
48.5
|
1.0
|
O2B
|
A:ATP303
|
3.3
|
52.3
|
1.0
|
O3G
|
A:ATP303
|
3.3
|
60.1
|
1.0
|
PG
|
A:ATP303
|
3.3
|
49.3
|
1.0
|
O3A
|
A:ATP303
|
3.6
|
46.6
|
1.0
|
CG
|
A:ASP853
|
3.6
|
40.4
|
1.0
|
ND2
|
A:ASN840
|
3.7
|
38.6
|
1.0
|
O1G
|
A:ATP303
|
4.0
|
52.5
|
1.0
|
O
|
A:MET839
|
4.1
|
35.8
|
1.0
|
O2'
|
A:ATP303
|
4.1
|
40.7
|
1.0
|
MG
|
A:MG305
|
4.1
|
27.7
|
1.0
|
O1A
|
A:ATP303
|
4.2
|
47.6
|
1.0
|
C2'
|
A:ATP303
|
4.2
|
37.9
|
1.0
|
CB
|
A:ASP853
|
4.3
|
31.5
|
1.0
|
PA
|
A:ATP303
|
4.5
|
46.2
|
1.0
|
CB
|
A:ASN840
|
4.6
|
27.5
|
1.0
|
OD1
|
A:ASP853
|
4.6
|
37.3
|
1.0
|
O2G
|
A:ATP303
|
4.6
|
52.0
|
1.0
|
C
|
A:MET839
|
4.6
|
32.6
|
1.0
|
C3'
|
A:ATP303
|
4.7
|
35.9
|
1.0
|
CA
|
A:ASN840
|
4.7
|
27.0
|
1.0
|
O1B
|
A:ATP303
|
4.8
|
63.2
|
1.0
|
N
|
A:ASN840
|
5.0
|
30.8
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 1zyd
Go back to
Magnesium Binding Sites List in 1zyd
Magnesium binding site 3 out
of 4 in the Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg307
b:22.6
occ:1.00
|
O1A
|
B:ATP304
|
2.1
|
47.4
|
1.0
|
OD2
|
B:ASP853
|
2.3
|
33.9
|
1.0
|
OD1
|
B:ASP853
|
2.7
|
48.0
|
1.0
|
CG
|
B:ASP853
|
2.8
|
36.6
|
1.0
|
O3G
|
B:ATP304
|
2.8
|
62.5
|
1.0
|
O3B
|
B:ATP304
|
3.0
|
56.5
|
1.0
|
O2G
|
B:ATP304
|
3.1
|
59.8
|
1.0
|
PG
|
B:ATP304
|
3.2
|
52.4
|
1.0
|
PA
|
B:ATP304
|
3.5
|
49.2
|
1.0
|
MG
|
B:MG308
|
4.1
|
42.2
|
1.0
|
O3A
|
B:ATP304
|
4.1
|
52.1
|
1.0
|
O2A
|
B:ATP304
|
4.2
|
47.9
|
1.0
|
NZ
|
B:LYS628
|
4.3
|
54.8
|
1.0
|
CB
|
B:ASP853
|
4.3
|
37.0
|
1.0
|
PB
|
B:ATP304
|
4.3
|
55.5
|
1.0
|
O
|
B:ASP853
|
4.4
|
36.6
|
1.0
|
OD2
|
B:ASP835
|
4.6
|
50.7
|
1.0
|
O5'
|
B:ATP304
|
4.6
|
50.7
|
1.0
|
O1G
|
B:ATP304
|
4.7
|
58.3
|
1.0
|
O
|
B:PHE854
|
4.9
|
37.9
|
1.0
|
O1B
|
B:ATP304
|
4.9
|
61.6
|
1.0
|
C
|
B:ASP853
|
4.9
|
37.1
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 1zyd
Go back to
Magnesium Binding Sites List in 1zyd
Magnesium binding site 4 out
of 4 in the Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: Wild-Type Complexed with Atp. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg308
b:42.2
occ:1.00
|
OD1
|
B:ASN840
|
2.1
|
40.9
|
1.0
|
O3B
|
B:ATP304
|
2.4
|
56.5
|
1.0
|
OD2
|
B:ASP853
|
2.7
|
33.9
|
1.0
|
O3G
|
B:ATP304
|
3.2
|
62.5
|
1.0
|
PG
|
B:ATP304
|
3.2
|
52.4
|
1.0
|
CG
|
B:ASN840
|
3.3
|
41.1
|
1.0
|
CG
|
B:ASP853
|
3.5
|
36.6
|
1.0
|
PB
|
B:ATP304
|
3.5
|
55.5
|
1.0
|
O2B
|
B:ATP304
|
3.6
|
54.5
|
1.0
|
O1G
|
B:ATP304
|
3.7
|
58.3
|
1.0
|
O3A
|
B:ATP304
|
3.8
|
52.1
|
1.0
|
ND2
|
B:ASN840
|
3.8
|
42.3
|
1.0
|
CB
|
B:ASP853
|
4.0
|
37.0
|
1.0
|
MG
|
B:MG307
|
4.1
|
22.6
|
1.0
|
O
|
B:MET839
|
4.1
|
45.4
|
1.0
|
O1A
|
B:ATP304
|
4.2
|
47.4
|
1.0
|
OD1
|
B:ASP853
|
4.3
|
48.0
|
1.0
|
C2'
|
B:ATP304
|
4.3
|
41.8
|
1.0
|
O2'
|
B:ATP304
|
4.4
|
49.6
|
1.0
|
CB
|
B:ASN840
|
4.5
|
32.8
|
1.0
|
O2G
|
B:ATP304
|
4.6
|
59.8
|
1.0
|
PA
|
B:ATP304
|
4.6
|
49.2
|
1.0
|
C
|
B:MET839
|
4.6
|
43.4
|
1.0
|
CA
|
B:ASN840
|
4.7
|
35.9
|
1.0
|
CE
|
B:LYS837
|
4.8
|
39.2
|
1.0
|
C3'
|
B:ATP304
|
4.9
|
43.4
|
1.0
|
N
|
B:ASN840
|
4.9
|
40.2
|
1.0
|
O1B
|
B:ATP304
|
4.9
|
61.6
|
1.0
|
|
Reference:
A.K.Padyana,
H.Qiu,
A.Roll-Mecak,
A.G.Hinnebusch,
S.K.Burley.
Structural Basis For Autoinhibition and Mutational Activation of Eukaryotic Initiation Factor 2{Alpha} Protein Kinase GCN2 J.Biol.Chem. V. 280 29289 2005.
ISSN: ISSN 0021-9258
PubMed: 15964839
DOI: 10.1074/JBC.M504096200
Page generated: Tue Aug 13 20:16:12 2024
|