Magnesium in PDB 2pz5: Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome
Enzymatic activity of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome
All present enzymatic activity of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome:
2.7.10.1;
Protein crystallography data
The structure of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome, PDB code: 2pz5
was solved by
H.Chen,
M.Mohammadi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
25.00 /
2.40
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
105.043,
114.474,
64.347,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.4 /
25.4
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome
(pdb code 2pz5). 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 Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome, PDB code: 2pz5:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 2pz5
Go back to
Magnesium Binding Sites List in 2pz5
Magnesium binding site 1 out
of 4 in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome
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 Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg301
b:2.0
occ:1.00
|
OD2
|
A:ASP644
|
2.2
|
22.6
|
1.0
|
ND2
|
A:ASN631
|
2.2
|
12.3
|
1.0
|
O1A
|
A:ACP300
|
2.2
|
17.0
|
1.0
|
O
|
A:HOH64
|
2.4
|
26.0
|
1.0
|
O3G
|
A:ACP300
|
2.4
|
14.9
|
1.0
|
O
|
A:HOH11
|
2.4
|
18.6
|
1.0
|
CG
|
A:ASP644
|
3.3
|
21.9
|
1.0
|
CG
|
A:ASN631
|
3.3
|
12.6
|
1.0
|
PG
|
A:ACP300
|
3.4
|
17.3
|
1.0
|
PA
|
A:ACP300
|
3.5
|
18.7
|
1.0
|
OD1
|
A:ASN631
|
3.6
|
12.1
|
1.0
|
O2G
|
A:ACP300
|
3.6
|
14.1
|
1.0
|
CB
|
A:ASP644
|
3.7
|
20.0
|
1.0
|
O3A
|
A:ACP300
|
3.8
|
16.6
|
1.0
|
MG
|
A:MG302
|
4.2
|
2.0
|
1.0
|
O
|
A:HOH155
|
4.2
|
33.2
|
1.0
|
C3B
|
A:ACP300
|
4.3
|
16.1
|
1.0
|
O
|
A:HOH82
|
4.3
|
21.6
|
1.0
|
O
|
A:HOH121
|
4.3
|
25.0
|
1.0
|
O1B
|
A:ACP300
|
4.3
|
13.1
|
1.0
|
OD1
|
A:ASP644
|
4.3
|
24.2
|
1.0
|
O
|
A:ARG630
|
4.4
|
15.1
|
1.0
|
PB
|
A:ACP300
|
4.4
|
16.7
|
1.0
|
O2A
|
A:ACP300
|
4.4
|
16.3
|
1.0
|
O5'
|
A:ACP300
|
4.5
|
17.2
|
1.0
|
OD1
|
A:ASP626
|
4.6
|
13.7
|
1.0
|
CB
|
A:ASN631
|
4.6
|
12.0
|
1.0
|
NE
|
A:ARG630
|
4.6
|
24.3
|
1.0
|
O1G
|
A:ACP300
|
4.6
|
18.1
|
1.0
|
C5'
|
A:ACP300
|
4.7
|
18.7
|
1.0
|
CA
|
A:ASN631
|
4.8
|
12.4
|
1.0
|
C
|
A:ARG630
|
4.9
|
14.7
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 2pz5
Go back to
Magnesium Binding Sites List in 2pz5
Magnesium binding site 2 out
of 4 in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome
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 Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg302
b:2.0
occ:1.00
|
O1B
|
A:ACP300
|
2.2
|
13.1
|
1.0
|
O2G
|
A:ACP300
|
2.3
|
14.1
|
1.0
|
O
|
A:HOH65
|
2.4
|
22.9
|
1.0
|
O
|
A:HOH2
|
2.4
|
32.2
|
1.0
|
OD1
|
A:ASP644
|
2.5
|
24.2
|
1.0
|
OD2
|
A:ASP644
|
2.6
|
22.6
|
1.0
|
CG
|
A:ASP644
|
2.9
|
21.9
|
1.0
|
PB
|
A:ACP300
|
3.4
|
16.7
|
1.0
|
PG
|
A:ACP300
|
3.4
|
17.3
|
1.0
|
C3B
|
A:ACP300
|
3.6
|
16.1
|
1.0
|
O
|
A:HOH14
|
3.8
|
27.0
|
1.0
|
O3G
|
A:ACP300
|
4.1
|
14.9
|
1.0
|
O
|
A:HOH82
|
4.1
|
21.6
|
1.0
|
MG
|
A:MG301
|
4.2
|
2.0
|
1.0
|
NZ
|
A:LYS517
|
4.3
|
20.4
|
1.0
|
O3A
|
A:ACP300
|
4.3
|
16.6
|
1.0
|
CA
|
A:GLY646
|
4.3
|
16.7
|
1.0
|
O
|
A:HOH51
|
4.4
|
19.9
|
1.0
|
CB
|
A:ASP644
|
4.4
|
20.0
|
1.0
|
O2B
|
A:ACP300
|
4.6
|
15.0
|
1.0
|
O1G
|
A:ACP300
|
4.6
|
18.1
|
1.0
|
N
|
A:GLY646
|
4.6
|
16.7
|
1.0
|
O1A
|
A:ACP300
|
4.7
|
17.0
|
1.0
|
O
|
A:HOH11
|
4.7
|
18.6
|
1.0
|
PA
|
A:ACP300
|
4.8
|
18.7
|
1.0
|
OD1
|
A:ASP626
|
4.8
|
13.7
|
1.0
|
O2A
|
A:ACP300
|
4.8
|
16.3
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 2pz5
Go back to
Magnesium Binding Sites List in 2pz5
Magnesium binding site 3 out
of 4 in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome
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 Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg301
b:2.0
occ:1.00
|
O2G
|
B:ACP300
|
2.2
|
17.9
|
1.0
|
OD2
|
B:ASP644
|
2.3
|
13.7
|
1.0
|
O2A
|
B:ACP300
|
2.3
|
13.8
|
1.0
|
ND2
|
B:ASN631
|
2.3
|
7.7
|
1.0
|
O
|
B:HOH78
|
2.3
|
25.2
|
1.0
|
O
|
B:HOH91
|
2.5
|
23.4
|
1.0
|
CG
|
B:ASP644
|
3.3
|
13.3
|
1.0
|
PG
|
B:ACP300
|
3.4
|
16.9
|
1.0
|
CG
|
B:ASN631
|
3.4
|
9.3
|
1.0
|
PA
|
B:ACP300
|
3.5
|
12.4
|
1.0
|
O3A
|
B:ACP300
|
3.6
|
12.9
|
1.0
|
O1G
|
B:ACP300
|
3.6
|
18.2
|
1.0
|
CB
|
B:ASP644
|
3.7
|
12.8
|
1.0
|
OD1
|
B:ASN631
|
3.8
|
10.3
|
1.0
|
MG
|
B:MG302
|
4.1
|
2.0
|
1.0
|
O
|
B:HOH145
|
4.2
|
17.5
|
1.0
|
O1B
|
B:ACP300
|
4.2
|
14.0
|
1.0
|
C3B
|
B:ACP300
|
4.2
|
15.9
|
1.0
|
PB
|
B:ACP300
|
4.3
|
13.9
|
1.0
|
OD1
|
B:ASP644
|
4.3
|
13.1
|
1.0
|
O
|
B:ARG630
|
4.4
|
11.0
|
1.0
|
O5'
|
B:ACP300
|
4.5
|
15.4
|
1.0
|
O1A
|
B:ACP300
|
4.5
|
13.1
|
1.0
|
O3G
|
B:ACP300
|
4.5
|
18.9
|
1.0
|
CB
|
B:ASN631
|
4.7
|
10.5
|
1.0
|
C5'
|
B:ACP300
|
4.7
|
15.5
|
1.0
|
NE
|
B:ARG630
|
4.8
|
22.2
|
1.0
|
OD1
|
B:ASP626
|
4.8
|
13.1
|
1.0
|
CA
|
B:ASN631
|
4.9
|
10.3
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 2pz5
Go back to
Magnesium Binding Sites List in 2pz5
Magnesium binding site 4 out
of 4 in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome
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 Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549T Mutation Responsible For Pfeiffer Syndrome within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg302
b:2.0
occ:1.00
|
O1B
|
B:ACP300
|
2.3
|
14.0
|
1.0
|
O1G
|
B:ACP300
|
2.3
|
18.2
|
1.0
|
O
|
B:HOH79
|
2.3
|
23.2
|
1.0
|
O
|
B:HOH75
|
2.4
|
22.0
|
1.0
|
OD1
|
B:ASP644
|
2.4
|
13.1
|
1.0
|
OD2
|
B:ASP644
|
2.5
|
13.7
|
1.0
|
CG
|
B:ASP644
|
2.8
|
13.3
|
1.0
|
PG
|
B:ACP300
|
3.4
|
16.9
|
1.0
|
PB
|
B:ACP300
|
3.4
|
13.9
|
1.0
|
C3B
|
B:ACP300
|
3.6
|
15.9
|
1.0
|
O
|
B:HOH66
|
3.8
|
18.7
|
1.0
|
O2G
|
B:ACP300
|
3.9
|
17.9
|
1.0
|
O
|
B:HOH145
|
4.0
|
17.5
|
1.0
|
MG
|
B:MG301
|
4.1
|
2.0
|
1.0
|
O3A
|
B:ACP300
|
4.2
|
12.9
|
1.0
|
CB
|
B:ASP644
|
4.3
|
12.8
|
1.0
|
NZ
|
B:LYS517
|
4.3
|
16.8
|
1.0
|
CA
|
B:GLY646
|
4.4
|
13.7
|
1.0
|
O
|
B:HOH70
|
4.4
|
26.3
|
1.0
|
O2B
|
B:ACP300
|
4.6
|
13.8
|
1.0
|
O2A
|
B:ACP300
|
4.7
|
13.8
|
1.0
|
O3G
|
B:ACP300
|
4.7
|
18.9
|
1.0
|
N
|
B:GLY646
|
4.7
|
13.2
|
1.0
|
PA
|
B:ACP300
|
4.8
|
12.4
|
1.0
|
O
|
B:HOH91
|
4.9
|
23.4
|
1.0
|
O1A
|
B:ACP300
|
4.9
|
13.1
|
1.0
|
OE1
|
B:GLU534
|
4.9
|
22.6
|
1.0
|
|
Reference:
H.Chen,
J.Ma,
W.Li,
A.V.Eliseenkova,
C.Xu,
T.A.Neubert,
W.T.Miller,
M.Mohammadi.
A Molecular Brake in the Kinase Hinge Region Regulates the Activity of Receptor Tyrosine Kinases. Mol.Cell V. 27 717 2007.
ISSN: ISSN 1097-2765
PubMed: 17803937
DOI: 10.1016/J.MOLCEL.2007.06.028
Page generated: Wed Aug 14 02:21:42 2024
|