Magnesium in PDB 9bgf: Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac
Enzymatic activity of Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac
All present enzymatic activity of Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac:
2.7.8.17;
Other elements in 9bgf:
The structure of Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac
(pdb code 9bgf). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac, PDB code: 9bgf:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 9bgf
Go back to
Magnesium Binding Sites List in 9bgf
Magnesium binding site 1 out
of 4 in the Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1302
b:9.4
occ:1.00
|
O
|
A:GLU324
|
3.8
|
23.1
|
1.0
|
O
|
A:SER321
|
3.8
|
20.9
|
1.0
|
O1A
|
A:UD11303
|
4.1
|
15.5
|
1.0
|
O2A
|
A:UD11303
|
4.1
|
32.1
|
1.0
|
OD1
|
A:ASP407
|
4.3
|
6.0
|
1.0
|
CB
|
A:ASP1152
|
4.4
|
21.4
|
1.0
|
PA
|
A:UD11303
|
4.5
|
12.7
|
1.0
|
O
|
A:ARG322
|
4.5
|
18.5
|
1.0
|
C
|
A:ARG322
|
4.7
|
18.5
|
1.0
|
OE2
|
A:GLU328
|
4.7
|
28.6
|
1.0
|
OE1
|
A:GLU328
|
4.7
|
33.6
|
1.0
|
OD2
|
A:ASP1152
|
4.7
|
27.9
|
1.0
|
C
|
A:SER321
|
4.9
|
19.2
|
1.0
|
N
|
A:PHE323
|
4.9
|
14.1
|
1.0
|
N
|
A:GLU324
|
4.9
|
19.5
|
1.0
|
C
|
A:GLU324
|
5.0
|
23.6
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 9bgf
Go back to
Magnesium Binding Sites List in 9bgf
Magnesium binding site 2 out
of 4 in the Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1308
b:4.9
occ:1.00
|
OD1
|
A:ASN1151
|
2.0
|
16.3
|
1.0
|
O2B
|
A:UD11303
|
2.0
|
14.5
|
1.0
|
OD2
|
A:ASP408
|
2.2
|
17.9
|
1.0
|
O2A
|
A:UD11303
|
2.5
|
32.1
|
1.0
|
CG
|
A:ASN1151
|
2.9
|
16.8
|
1.0
|
CG
|
A:ASP408
|
3.2
|
11.4
|
1.0
|
PB
|
A:UD11303
|
3.4
|
5.8
|
1.0
|
ND2
|
A:ASN406
|
3.5
|
5.4
|
1.0
|
OD1
|
A:ASP408
|
3.5
|
10.2
|
1.0
|
ND2
|
A:ASN1151
|
3.6
|
28.6
|
1.0
|
PA
|
A:UD11303
|
3.6
|
12.7
|
1.0
|
CB
|
A:ASN1151
|
3.8
|
13.6
|
1.0
|
CA
|
A:ASN1151
|
3.9
|
11.8
|
1.0
|
O3A
|
A:UD11303
|
3.9
|
5.1
|
1.0
|
O1'
|
A:UD11303
|
4.2
|
10.2
|
1.0
|
O1A
|
A:UD11303
|
4.4
|
15.5
|
1.0
|
CB
|
A:ASP408
|
4.5
|
6.6
|
1.0
|
N
|
A:ASP1152
|
4.5
|
24.2
|
1.0
|
O1B
|
A:UD11303
|
4.6
|
8.0
|
1.0
|
SG
|
A:CYS1149
|
4.7
|
6.7
|
1.0
|
C
|
A:ASN1151
|
4.7
|
19.8
|
1.0
|
CG
|
A:ASN406
|
4.8
|
5.5
|
1.0
|
N
|
A:ASN1151
|
4.9
|
9.6
|
1.0
|
O5B
|
A:UD11303
|
4.9
|
5.2
|
1.0
|
O
|
A:LEU1150
|
5.0
|
12.9
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 9bgf
Go back to
Magnesium Binding Sites List in 9bgf
Magnesium binding site 3 out
of 4 in the Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1302
b:11.0
occ:1.00
|
OD1
|
B:ASN1151
|
1.9
|
10.9
|
1.0
|
OD2
|
B:ASP408
|
1.9
|
22.2
|
1.0
|
O2B
|
B:UD11303
|
2.0
|
16.1
|
1.0
|
O2A
|
B:UD11303
|
2.4
|
12.0
|
1.0
|
CG
|
B:ASN1151
|
3.1
|
11.9
|
1.0
|
CG
|
B:ASP408
|
3.1
|
17.4
|
1.0
|
PB
|
B:UD11303
|
3.3
|
4.7
|
1.0
|
OD1
|
B:ASN406
|
3.5
|
12.0
|
1.0
|
PA
|
B:UD11303
|
3.6
|
5.4
|
1.0
|
ND2
|
B:ASN1151
|
3.8
|
14.5
|
1.0
|
CB
|
B:ASP408
|
3.8
|
4.7
|
1.0
|
O3A
|
B:UD11303
|
3.9
|
4.2
|
1.0
|
OD1
|
B:ASP408
|
4.1
|
24.3
|
1.0
|
O1'
|
B:UD11303
|
4.2
|
12.5
|
1.0
|
CB
|
B:ASN1151
|
4.2
|
13.3
|
1.0
|
CA
|
B:ASN1151
|
4.3
|
11.2
|
1.0
|
O1A
|
B:UD11303
|
4.5
|
13.8
|
1.0
|
O1B
|
B:UD11303
|
4.5
|
3.5
|
1.0
|
CG
|
B:ASN406
|
4.7
|
9.5
|
1.0
|
O5B
|
B:UD11303
|
4.8
|
4.9
|
1.0
|
SG
|
B:CYS1149
|
4.8
|
4.1
|
1.0
|
O
|
B:ASN406
|
4.8
|
10.9
|
1.0
|
C5B
|
B:UD11303
|
4.9
|
4.6
|
1.0
|
N
|
B:ASP1152
|
4.9
|
19.0
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 9bgf
Go back to
Magnesium Binding Sites List in 9bgf
Magnesium binding site 4 out
of 4 in the Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Structure of Human Glcnac-1-Phosphotransferase Complexed with the Donor Substrate Udp-Glcnac within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1306
b:5.3
occ:1.00
|
OD1
|
B:ASP408
|
3.5
|
24.3
|
1.0
|
O
|
B:SER321
|
3.6
|
31.7
|
1.0
|
O
|
B:GLU324
|
3.8
|
14.8
|
1.0
|
O2A
|
B:UD11303
|
4.1
|
12.0
|
1.0
|
CB
|
B:ASP1152
|
4.2
|
19.8
|
1.0
|
OD2
|
B:ASP408
|
4.2
|
22.2
|
1.0
|
OE1
|
B:GLU328
|
4.3
|
18.1
|
1.0
|
CG
|
B:ASP408
|
4.3
|
17.4
|
1.0
|
O1A
|
B:UD11303
|
4.4
|
13.8
|
1.0
|
OD2
|
B:ASP407
|
4.5
|
7.1
|
1.0
|
OD2
|
B:ASP1152
|
4.5
|
21.6
|
1.0
|
O
|
B:ARG322
|
4.6
|
13.4
|
1.0
|
C
|
B:SER321
|
4.7
|
21.2
|
1.0
|
C
|
B:ARG322
|
4.7
|
13.2
|
1.0
|
PA
|
B:UD11303
|
4.7
|
5.4
|
1.0
|
OD1
|
B:ASN326
|
4.8
|
18.8
|
1.0
|
CG
|
B:ASP1152
|
4.9
|
20.7
|
1.0
|
N
|
B:GLU324
|
4.9
|
17.0
|
1.0
|
C
|
B:GLU324
|
5.0
|
17.1
|
1.0
|
CA
|
B:ARG322
|
5.0
|
15.6
|
1.0
|
|
Reference:
H.Li,
B.Doray,
B.C.Jennings,
W.S.Lee,
L.Liu,
S.Kornfeld,
H.Li.
Structure of A Truncated Human Glcnac-1-Phosphotransferase Variant Reveals the Basis For Its Hyperactivity. J.Biol.Chem. V. 300 07706 2024.
ISSN: ESSN 1083-351X
PubMed: 39178950
DOI: 10.1016/J.JBC.2024.107706
Page generated: Fri Aug 15 23:16:31 2025
|