Sodium in PDB 5ggp: Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide
Protein crystallography data
The structure of Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide, PDB code: 5ggp
was solved by
N.Kuwabara,
T.Senda,
R.Kato,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.55 /
1.60
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
111.113,
49.743,
61.716,
90.00,
105.89,
90.00
|
R / Rfree (%)
|
21.6 /
24.6
|
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide
(pdb code 5ggp). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 5 binding sites of Sodium where determined in the
Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide, PDB code: 5ggp:
Jump to Sodium binding site number:
1;
2;
3;
4;
5;
Sodium binding site 1 out
of 5 in 5ggp
Go back to
Sodium Binding Sites List in 5ggp
Sodium binding site 1 out
of 5 in the Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na301
b:10.3
occ:1.00
|
OG
|
A:SER232
|
3.0
|
13.1
|
1.0
|
O3
|
C:MAN101
|
3.2
|
14.3
|
1.0
|
NH2
|
A:ARG207
|
3.4
|
13.2
|
1.0
|
O4
|
C:MAN101
|
3.6
|
18.6
|
1.0
|
CB
|
A:SER232
|
3.7
|
12.7
|
1.0
|
CA
|
A:SER232
|
3.9
|
13.5
|
1.0
|
NH1
|
A:ARG207
|
4.3
|
12.7
|
1.0
|
CZ
|
A:ARG207
|
4.3
|
11.8
|
1.0
|
C3
|
C:MAN101
|
4.3
|
15.2
|
1.0
|
C4
|
C:MAN101
|
4.3
|
18.2
|
1.0
|
O
|
A:LEU231
|
4.5
|
11.9
|
1.0
|
N
|
A:SER232
|
4.7
|
12.4
|
1.0
|
C
|
A:LEU231
|
4.9
|
12.4
|
1.0
|
C
|
A:SER232
|
5.0
|
15.1
|
1.0
|
|
Sodium binding site 2 out
of 5 in 5ggp
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Sodium Binding Sites List in 5ggp
Sodium binding site 2 out
of 5 in the Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na302
b:18.1
occ:1.00
|
O
|
A:HOH514
|
2.7
|
17.4
|
1.0
|
O
|
A:GLY235
|
2.8
|
13.4
|
1.0
|
N
|
A:ARG107
|
2.9
|
9.7
|
1.0
|
CG
|
A:PRO237
|
3.5
|
12.1
|
1.0
|
CA
|
A:SER106
|
3.5
|
12.8
|
1.0
|
CD
|
A:PRO237
|
3.5
|
12.1
|
1.0
|
CB
|
A:ARG107
|
3.6
|
10.5
|
1.0
|
C
|
A:SER106
|
3.7
|
10.0
|
1.0
|
CB
|
A:SER106
|
3.7
|
12.7
|
1.0
|
N
|
A:PRO237
|
3.7
|
11.6
|
1.0
|
O
|
A:HOH492
|
3.7
|
20.3
|
1.0
|
O
|
A:HOH495
|
3.8
|
20.0
|
1.0
|
CA
|
A:ARG107
|
3.8
|
14.0
|
1.0
|
CG2
|
A:THR209
|
3.8
|
11.0
|
1.0
|
CB
|
A:TRP234
|
4.0
|
12.2
|
1.0
|
C
|
A:GLY235
|
4.0
|
12.3
|
1.0
|
CA
|
A:PRO237
|
4.1
|
10.6
|
1.0
|
C
|
A:ASP236
|
4.2
|
12.9
|
1.0
|
CB
|
A:PRO237
|
4.3
|
12.0
|
1.0
|
CA
|
A:ASP236
|
4.6
|
13.6
|
1.0
|
O
|
A:ASP236
|
4.7
|
12.2
|
1.0
|
OG
|
A:SER106
|
4.7
|
11.7
|
1.0
|
CG
|
A:TRP234
|
4.8
|
12.5
|
1.0
|
N
|
A:ASP236
|
4.8
|
11.0
|
1.0
|
O
|
A:SER106
|
4.9
|
9.4
|
1.0
|
N
|
A:SER106
|
4.9
|
10.4
|
1.0
|
C
|
A:TRP234
|
4.9
|
12.8
|
1.0
|
N
|
A:GLY235
|
4.9
|
11.5
|
1.0
|
|
Sodium binding site 3 out
of 5 in 5ggp
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Sodium Binding Sites List in 5ggp
Sodium binding site 3 out
of 5 in the Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 3 of Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na301
b:13.8
occ:1.00
|
N
|
B:HIS155
|
3.2
|
16.4
|
1.0
|
NZ
|
B:LYS186
|
3.3
|
18.2
|
1.0
|
CD2
|
B:HIS184
|
3.6
|
18.8
|
1.0
|
CA
|
B:PRO154
|
3.7
|
14.6
|
1.0
|
CB
|
B:HIS184
|
3.9
|
12.4
|
1.0
|
CD
|
B:LYS186
|
3.9
|
20.0
|
1.0
|
ND1
|
B:HIS155
|
4.0
|
21.3
|
1.0
|
C
|
B:PRO154
|
4.0
|
17.6
|
1.0
|
CE
|
B:LYS186
|
4.0
|
20.8
|
1.0
|
CG
|
B:HIS184
|
4.0
|
16.2
|
1.0
|
CA
|
B:HIS155
|
4.1
|
14.6
|
1.0
|
CE1
|
B:HIS155
|
4.1
|
25.1
|
1.0
|
CB
|
B:PRO154
|
4.2
|
17.6
|
1.0
|
CG
|
B:HIS155
|
4.2
|
19.8
|
1.0
|
CG
|
B:LYS186
|
4.2
|
18.2
|
1.0
|
O
|
B:HIS184
|
4.3
|
14.6
|
1.0
|
OD1
|
B:ASP157
|
4.3
|
14.3
|
1.0
|
NE2
|
B:HIS155
|
4.4
|
24.2
|
1.0
|
CD2
|
B:HIS155
|
4.5
|
21.5
|
1.0
|
OE2
|
B:GLU158
|
4.6
|
21.2
|
1.0
|
CA
|
B:HIS184
|
4.7
|
13.4
|
1.0
|
CB
|
B:HIS155
|
4.8
|
16.8
|
1.0
|
NE2
|
B:HIS184
|
4.8
|
20.4
|
1.0
|
C
|
B:HIS184
|
4.9
|
13.5
|
1.0
|
N
|
B:PRO154
|
5.0
|
17.9
|
1.0
|
O
|
B:HOH427
|
5.0
|
12.8
|
1.0
|
|
Sodium binding site 4 out
of 5 in 5ggp
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Sodium Binding Sites List in 5ggp
Sodium binding site 4 out
of 5 in the Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 4 of Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na302
b:8.6
occ:1.00
|
OG
|
B:SER232
|
3.0
|
12.2
|
1.0
|
O3
|
D:MAN101
|
3.2
|
14.9
|
1.0
|
NH2
|
B:ARG207
|
3.3
|
11.9
|
1.0
|
O4
|
D:MAN101
|
3.6
|
17.9
|
1.0
|
CB
|
B:SER232
|
3.7
|
13.9
|
1.0
|
CA
|
B:SER232
|
3.8
|
14.7
|
1.0
|
O
|
D:HOH212
|
4.3
|
22.4
|
1.0
|
CZ
|
B:ARG207
|
4.3
|
12.6
|
1.0
|
C4
|
D:MAN101
|
4.3
|
16.8
|
1.0
|
C3
|
D:MAN101
|
4.3
|
13.9
|
1.0
|
NH1
|
B:ARG207
|
4.3
|
13.0
|
1.0
|
O
|
B:LEU231
|
4.5
|
14.1
|
1.0
|
O
|
B:HOH467
|
4.5
|
23.8
|
1.0
|
N
|
B:SER232
|
4.7
|
11.4
|
1.0
|
C
|
B:LEU231
|
4.9
|
11.5
|
1.0
|
C
|
B:SER232
|
4.9
|
14.4
|
1.0
|
O
|
D:HOH220
|
5.0
|
33.7
|
1.0
|
|
Sodium binding site 5 out
of 5 in 5ggp
Go back to
Sodium Binding Sites List in 5ggp
Sodium binding site 5 out
of 5 in the Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 5 of Crystal Structure of N-Terminal Domain of Human Protein O-Mannose Beta-1,2-N-Acetylglucosaminyltransferase in Complex with Glcnac- BETA1,2-Man-Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na303
b:19.9
occ:1.00
|
NE
|
B:ARG171
|
3.2
|
20.0
|
1.0
|
N
|
B:ALA168
|
3.3
|
15.2
|
1.0
|
CG
|
B:ARG171
|
3.6
|
16.6
|
1.0
|
O
|
B:HOH519
|
3.7
|
52.9
|
1.0
|
CB
|
B:ALA168
|
3.9
|
10.5
|
1.0
|
CA
|
B:VAL167
|
3.9
|
12.4
|
1.0
|
CD
|
B:ARG171
|
4.0
|
17.8
|
1.0
|
C
|
B:VAL167
|
4.1
|
15.5
|
1.0
|
NH2
|
B:ARG171
|
4.1
|
16.7
|
1.0
|
CZ
|
B:ARG171
|
4.1
|
20.2
|
1.0
|
CE
|
B:MET144
|
4.2
|
19.2
|
1.0
|
CA
|
B:ALA168
|
4.2
|
15.4
|
1.0
|
O
|
B:MET166
|
4.2
|
18.0
|
1.0
|
CG1
|
B:VAL167
|
4.3
|
12.1
|
1.0
|
SD
|
B:MET144
|
4.6
|
15.2
|
1.0
|
CB
|
B:VAL167
|
4.6
|
13.8
|
1.0
|
CB
|
B:ARG171
|
4.9
|
14.7
|
1.0
|
N
|
B:VAL167
|
5.0
|
14.1
|
1.0
|
|
Reference:
N.Kuwabara,
H.Manya,
T.Yamada,
H.Tateno,
M.Kanagawa,
K.Kobayashi,
K.Akasaka-Manya,
Y.Hirose,
M.Mizuno,
M.Ikeguchi,
T.Toda,
J.Hirabayashi,
T.Senda,
T.Endo,
R.Kato.
Carbohydrate-Binding Domain of the POMGNT1 Stem Region Modulates O-Mannosylation Sites of Alpha-Dystroglycan Proc.Natl.Acad.Sci.Usa V. 113 9280 2016.
ISSN: ESSN 1091-6490
PubMed: 27493216
DOI: 10.1073/PNAS.1525545113
Page generated: Mon Oct 7 21:10:15 2024
|