Cobalt in PDB 5v7y: Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Protein crystallography data
The structure of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu, PDB code: 5v7y
was solved by
N.J.Schnicker,
M.Dey,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
63.40 /
2.05
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
50.238,
106.826,
81.056,
90.00,
103.65,
90.00
|
R / Rfree (%)
|
16.1 /
20.9
|
Other elements in 5v7y:
The structure of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu also contains other interesting chemical elements:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
(pdb code 5v7y). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 4 binding sites of Cobalt where determined in the
Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu, PDB code: 5v7y:
Jump to Cobalt binding site number:
1;
2;
3;
4;
Cobalt binding site 1 out
of 4 in 5v7y
Go back to
Cobalt Binding Sites List in 5v7y
Cobalt binding site 1 out
of 4 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 1 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Co301
b:15.0
occ:1.00
|
N3
|
A:IMD302
|
2.0
|
16.2
|
1.0
|
NE2
|
A:HIS193
|
2.0
|
14.5
|
1.0
|
OD1
|
A:ASP129
|
2.0
|
13.7
|
1.0
|
NE2
|
A:HIS127
|
2.1
|
16.1
|
1.0
|
C4
|
A:IMD302
|
2.7
|
20.0
|
1.0
|
CG
|
A:ASP129
|
2.9
|
16.0
|
1.0
|
CE1
|
A:HIS193
|
2.9
|
13.8
|
1.0
|
CD2
|
A:HIS127
|
2.9
|
17.0
|
1.0
|
OD2
|
A:ASP129
|
3.0
|
12.6
|
1.0
|
CD2
|
A:HIS193
|
3.1
|
15.9
|
1.0
|
CE1
|
A:HIS127
|
3.1
|
18.0
|
1.0
|
C2
|
A:IMD302
|
3.2
|
18.9
|
1.0
|
C5
|
A:IMD302
|
4.0
|
18.7
|
1.0
|
ND1
|
A:HIS193
|
4.1
|
12.5
|
1.0
|
CG
|
A:HIS127
|
4.1
|
20.4
|
1.0
|
ND1
|
A:HIS127
|
4.1
|
14.8
|
1.0
|
CG
|
A:HIS193
|
4.2
|
15.1
|
1.0
|
N1
|
A:IMD302
|
4.2
|
12.6
|
1.0
|
O
|
A:HOH534
|
4.3
|
30.3
|
1.0
|
CB
|
A:ASP129
|
4.3
|
13.2
|
1.0
|
F3
|
A:TFA303
|
4.5
|
26.9
|
1.0
|
NE1
|
A:TRP209
|
4.6
|
14.0
|
1.0
|
CA
|
A:ASP129
|
4.7
|
16.6
|
1.0
|
N
|
A:ASP129
|
4.8
|
13.7
|
1.0
|
CZ
|
A:PHE178
|
4.8
|
8.8
|
1.0
|
F2
|
A:TFA303
|
4.8
|
37.9
|
1.0
|
O
|
A:HIS193
|
4.9
|
16.4
|
1.0
|
O
|
A:HIS127
|
5.0
|
17.1
|
1.0
|
|
Cobalt binding site 2 out
of 4 in 5v7y
Go back to
Cobalt Binding Sites List in 5v7y
Cobalt binding site 2 out
of 4 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 2 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Co301
b:13.6
occ:1.00
|
O1
|
B:AKG302
|
2.0
|
16.2
|
1.0
|
OD1
|
B:ASP129
|
2.0
|
8.8
|
1.0
|
NE2
|
B:HIS193
|
2.1
|
11.8
|
1.0
|
NE2
|
B:HIS127
|
2.1
|
17.9
|
1.0
|
O5
|
B:AKG302
|
2.4
|
18.8
|
1.0
|
CG
|
B:ASP129
|
2.8
|
15.9
|
1.0
|
C1
|
B:AKG302
|
2.8
|
14.7
|
1.0
|
CE1
|
B:HIS193
|
2.9
|
11.7
|
1.0
|
CE1
|
B:HIS127
|
3.0
|
16.0
|
1.0
|
OD2
|
B:ASP129
|
3.0
|
11.3
|
1.0
|
C2
|
B:AKG302
|
3.0
|
16.3
|
1.0
|
CD2
|
B:HIS127
|
3.1
|
10.9
|
1.0
|
CD2
|
B:HIS193
|
3.1
|
7.3
|
1.0
|
O
|
B:HOH491
|
3.6
|
18.4
|
1.0
|
ND1
|
B:HIS193
|
4.0
|
11.2
|
1.0
|
O2
|
B:AKG302
|
4.0
|
12.3
|
1.0
|
ND1
|
B:HIS127
|
4.1
|
14.0
|
1.0
|
CG
|
B:HIS193
|
4.2
|
8.9
|
1.0
|
CG
|
B:HIS127
|
4.2
|
15.2
|
1.0
|
CB
|
B:ASP129
|
4.3
|
11.3
|
1.0
|
CE2
|
B:TYR124
|
4.4
|
19.1
|
1.0
|
NE1
|
B:TRP209
|
4.4
|
10.3
|
1.0
|
C3
|
B:AKG302
|
4.5
|
17.1
|
1.0
|
OH
|
B:TYR124
|
4.7
|
20.0
|
1.0
|
CA
|
B:ASP129
|
4.7
|
11.1
|
1.0
|
CZ
|
B:TYR124
|
4.7
|
22.1
|
1.0
|
CZ
|
B:PHE178
|
4.8
|
10.4
|
1.0
|
N
|
B:ASP129
|
4.8
|
14.6
|
1.0
|
|
Cobalt binding site 3 out
of 4 in 5v7y
Go back to
Cobalt Binding Sites List in 5v7y
Cobalt binding site 3 out
of 4 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 3 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Co301
b:12.1
occ:1.00
|
N1
|
D:IMD302
|
1.9
|
17.8
|
1.0
|
OD1
|
D:ASP129
|
2.0
|
12.3
|
1.0
|
NE2
|
D:HIS193
|
2.0
|
13.6
|
1.0
|
NE2
|
D:HIS127
|
2.1
|
13.3
|
1.0
|
OD2
|
D:ASP129
|
2.5
|
12.5
|
1.0
|
CG
|
D:ASP129
|
2.6
|
14.1
|
1.0
|
C5
|
D:IMD302
|
2.9
|
23.4
|
1.0
|
C2
|
D:IMD302
|
3.0
|
12.8
|
1.0
|
CD2
|
D:HIS193
|
3.0
|
10.8
|
1.0
|
CE1
|
D:HIS127
|
3.0
|
13.8
|
1.0
|
CE1
|
D:HIS193
|
3.0
|
12.0
|
1.0
|
CD2
|
D:HIS127
|
3.0
|
12.9
|
1.0
|
CB
|
D:ASP129
|
4.1
|
14.4
|
1.0
|
ND1
|
D:HIS127
|
4.1
|
15.5
|
1.0
|
N3
|
D:IMD302
|
4.1
|
12.6
|
1.0
|
C4
|
D:IMD302
|
4.1
|
17.3
|
1.0
|
ND1
|
D:HIS193
|
4.1
|
11.7
|
1.0
|
CG
|
D:HIS193
|
4.1
|
12.0
|
1.0
|
CG
|
D:HIS127
|
4.1
|
17.1
|
1.0
|
NE1
|
D:TRP209
|
4.4
|
12.5
|
1.0
|
O
|
D:HOH527
|
4.5
|
28.7
|
1.0
|
F1
|
D:TFA305
|
4.6
|
22.3
|
0.7
|
CA
|
D:ASP129
|
4.6
|
13.0
|
1.0
|
N
|
D:ASP129
|
4.7
|
11.5
|
1.0
|
CZ
|
D:PHE178
|
4.8
|
8.9
|
1.0
|
F3
|
D:TFA305
|
4.8
|
26.2
|
0.7
|
O
|
D:HIS127
|
5.0
|
12.2
|
1.0
|
CZ2
|
D:TRP209
|
5.0
|
14.1
|
1.0
|
|
Cobalt binding site 4 out
of 4 in 5v7y
Go back to
Cobalt Binding Sites List in 5v7y
Cobalt binding site 4 out
of 4 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 4 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Co301
b:16.2
occ:1.00
|
N1
|
C:IMD302
|
1.9
|
10.7
|
1.0
|
NE2
|
C:HIS193
|
2.0
|
19.0
|
1.0
|
OD1
|
C:ASP129
|
2.1
|
20.0
|
1.0
|
NE2
|
C:HIS127
|
2.1
|
20.1
|
1.0
|
OD2
|
C:ASP129
|
2.4
|
16.9
|
1.0
|
C5
|
C:IMD302
|
2.5
|
21.0
|
1.0
|
CG
|
C:ASP129
|
2.6
|
16.0
|
1.0
|
CE1
|
C:HIS193
|
2.9
|
17.6
|
1.0
|
CE1
|
C:HIS127
|
3.0
|
18.2
|
1.0
|
CD2
|
C:HIS127
|
3.0
|
16.6
|
1.0
|
CD2
|
C:HIS193
|
3.0
|
15.1
|
1.0
|
C2
|
C:IMD302
|
3.2
|
19.7
|
1.0
|
C4
|
C:IMD302
|
3.8
|
18.2
|
1.0
|
ND1
|
C:HIS193
|
4.0
|
14.7
|
1.0
|
CB
|
C:ASP129
|
4.1
|
16.2
|
1.0
|
ND1
|
C:HIS127
|
4.1
|
16.2
|
1.0
|
N3
|
C:IMD302
|
4.1
|
14.1
|
1.0
|
CG
|
C:HIS193
|
4.1
|
20.1
|
1.0
|
CG
|
C:HIS127
|
4.1
|
18.6
|
1.0
|
F2
|
C:TFA303
|
4.6
|
32.2
|
1.0
|
F3
|
C:TFA303
|
4.6
|
29.4
|
1.0
|
CA
|
C:ASP129
|
4.7
|
17.1
|
1.0
|
CZ
|
C:PHE178
|
4.7
|
14.9
|
1.0
|
NE1
|
C:TRP209
|
4.7
|
16.8
|
1.0
|
N
|
C:ASP129
|
4.8
|
14.6
|
1.0
|
F1
|
C:TFA303
|
4.9
|
28.6
|
1.0
|
C2
|
C:TFA303
|
5.0
|
23.9
|
1.0
|
|
Reference:
N.J.Schnicker,
M.Razzaghi,
S.Guha Thakurta,
S.Chakravarthy,
M.Dey.
Bacillus Anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu. Biochemistry V. 56 5771 2017.
ISSN: ISSN 1520-4995
PubMed: 28981257
DOI: 10.1021/ACS.BIOCHEM.7B00601
Page generated: Tue Jul 30 18:15:58 2024
|