Manganese in PDB 8vh8: Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A
Protein crystallography data
The structure of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A, PDB code: 8vh8
was solved by
L.C.Pedersen,
J.Liu,
E.Stancanelli,
J.M.Krahn,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
28.76 /
2.85
|
Space group
|
P 43
|
Cell size a, b, c (Å), α, β, γ (°)
|
118.57,
118.57,
262.356,
90,
90,
90
|
R / Rfree (%)
|
19.8 /
22.3
|
Other elements in 8vh8:
The structure of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A
(pdb code 8vh8). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 8 binding sites of Manganese where determined in the
Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A, PDB code: 8vh8:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Manganese binding site 1 out
of 8 in 8vh8
Go back to
Manganese Binding Sites List in 8vh8
Manganese binding site 1 out
of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn701
b:110.9
occ:1.00
|
OD2
|
A:ASP481
|
2.1
|
114.8
|
1.0
|
O2A
|
A:UDP702
|
2.1
|
111.4
|
1.0
|
O1B
|
A:UDP702
|
2.2
|
110.4
|
1.0
|
O
|
A:HOH801
|
2.2
|
105.0
|
1.0
|
CG
|
A:ASP481
|
3.0
|
112.4
|
1.0
|
OD1
|
A:ASP481
|
3.3
|
109.4
|
1.0
|
PB
|
A:UDP702
|
3.3
|
110.7
|
1.0
|
PA
|
A:UDP702
|
3.4
|
111.4
|
1.0
|
O3A
|
A:UDP702
|
3.5
|
110.6
|
1.0
|
O3B
|
A:UDP702
|
3.9
|
109.8
|
1.0
|
H5'1
|
A:UDP702
|
3.9
|
132.7
|
1.0
|
HH22
|
A:ARG403
|
4.0
|
137.3
|
1.0
|
HH12
|
A:ARG403
|
4.1
|
137.4
|
1.0
|
OD2
|
A:ASP479
|
4.3
|
98.5
|
1.0
|
O1A
|
A:UDP702
|
4.3
|
111.6
|
1.0
|
CB
|
A:ASP481
|
4.4
|
112.4
|
1.0
|
O5'
|
A:UDP702
|
4.5
|
111.3
|
1.0
|
O2B
|
A:UDP702
|
4.6
|
110.8
|
1.0
|
C5'
|
A:UDP702
|
4.6
|
110.5
|
1.0
|
HB2
|
A:ASP481
|
4.6
|
134.9
|
1.0
|
NH2
|
A:ARG403
|
4.7
|
114.4
|
1.0
|
HB3
|
A:ASP479
|
4.7
|
118.0
|
1.0
|
HB3
|
A:ASP481
|
4.7
|
134.9
|
1.0
|
H5'2
|
A:UDP702
|
4.8
|
132.7
|
1.0
|
NH1
|
A:ARG403
|
4.8
|
114.5
|
1.0
|
|
Manganese binding site 2 out
of 8 in 8vh8
Go back to
Manganese Binding Sites List in 8vh8
Manganese binding site 2 out
of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn703
b:72.0
occ:1.00
|
O3B
|
A:UDP704
|
2.1
|
73.4
|
1.0
|
OD2
|
A:ASP217
|
2.1
|
70.2
|
1.0
|
O
|
A:HOH802
|
2.2
|
73.5
|
1.0
|
OD1
|
A:ASP217
|
2.2
|
68.4
|
1.0
|
O2A
|
A:UDP704
|
2.3
|
70.2
|
1.0
|
CG
|
A:ASP217
|
2.5
|
68.7
|
1.0
|
H5'1
|
A:UDP704
|
3.1
|
81.2
|
1.0
|
PB
|
A:UDP704
|
3.2
|
73.4
|
1.0
|
O3A
|
A:UDP704
|
3.3
|
71.1
|
1.0
|
PA
|
A:UDP704
|
3.3
|
70.4
|
1.0
|
HH12
|
A:ARG247
|
3.6
|
95.4
|
1.0
|
OD1
|
A:ASP218
|
3.6
|
74.6
|
1.0
|
OD1
|
A:ASN317
|
3.8
|
78.8
|
1.0
|
H3'
|
A:UDP704
|
3.8
|
78.9
|
1.0
|
HE
|
A:ARG320
|
3.8
|
86.3
|
1.0
|
OD2
|
A:ASP218
|
3.8
|
71.2
|
1.0
|
CB
|
A:ASP217
|
4.0
|
66.5
|
1.0
|
O1B
|
A:UDP704
|
4.0
|
74.2
|
1.0
|
C5'
|
A:UDP704
|
4.1
|
67.6
|
1.0
|
CG
|
A:ASP218
|
4.1
|
73.0
|
1.0
|
O5'
|
A:UDP704
|
4.2
|
67.3
|
1.0
|
HB3
|
A:ASP215
|
4.2
|
77.6
|
1.0
|
HH21
|
A:ARG320
|
4.3
|
83.7
|
1.0
|
HB3
|
A:ASP217
|
4.3
|
79.8
|
1.0
|
HB2
|
A:ASP215
|
4.3
|
77.6
|
1.0
|
O
|
A:THR318
|
4.4
|
79.9
|
1.0
|
HB2
|
A:ASP217
|
4.4
|
79.8
|
1.0
|
NH1
|
A:ARG247
|
4.4
|
79.5
|
1.0
|
O2B
|
A:UDP704
|
4.4
|
76.7
|
1.0
|
HB2
|
A:SER323
|
4.5
|
98.3
|
1.0
|
OD2
|
A:ASP215
|
4.6
|
66.7
|
1.0
|
HH22
|
A:ARG247
|
4.6
|
94.4
|
1.0
|
O1A
|
A:UDP704
|
4.6
|
71.8
|
1.0
|
H
|
A:ASP217
|
4.6
|
75.9
|
1.0
|
NE
|
A:ARG320
|
4.6
|
71.9
|
1.0
|
CB
|
A:ASP215
|
4.7
|
64.7
|
1.0
|
H5'2
|
A:UDP704
|
4.7
|
81.2
|
1.0
|
C3'
|
A:UDP704
|
4.8
|
65.8
|
1.0
|
HH11
|
A:ARG247
|
4.8
|
95.4
|
1.0
|
HG2
|
A:ARG320
|
4.8
|
94.7
|
1.0
|
H
|
A:THR318
|
4.9
|
92.1
|
1.0
|
CA
|
A:ASP217
|
5.0
|
64.2
|
1.0
|
C4'
|
A:UDP704
|
5.0
|
65.2
|
1.0
|
HB
|
A:THR318
|
5.0
|
91.1
|
1.0
|
CG
|
A:ASN317
|
5.0
|
79.0
|
1.0
|
|
Manganese binding site 3 out
of 8 in 8vh8
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Manganese Binding Sites List in 8vh8
Manganese binding site 3 out
of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn701
b:97.6
occ:1.00
|
O1B
|
B:UDP702
|
2.1
|
94.8
|
1.0
|
O
|
B:HOH802
|
2.1
|
91.0
|
1.0
|
OD2
|
B:ASP481
|
2.2
|
98.5
|
1.0
|
O2A
|
B:UDP702
|
2.2
|
94.1
|
1.0
|
CG
|
B:ASP481
|
3.1
|
94.3
|
1.0
|
PA
|
B:UDP702
|
3.3
|
94.3
|
1.0
|
PB
|
B:UDP702
|
3.4
|
95.0
|
1.0
|
OD1
|
B:ASP481
|
3.4
|
90.8
|
1.0
|
O3A
|
B:UDP702
|
3.5
|
94.0
|
1.0
|
O3B
|
B:UDP702
|
4.3
|
94.2
|
1.0
|
O1A
|
B:UDP702
|
4.3
|
94.4
|
1.0
|
O2B
|
B:UDP702
|
4.4
|
94.8
|
1.0
|
OD2
|
B:ASP479
|
4.4
|
88.6
|
1.0
|
CB
|
B:ASP481
|
4.5
|
96.3
|
1.0
|
O5'
|
B:UDP702
|
4.5
|
93.5
|
1.0
|
OE2
|
B:GLU595
|
4.5
|
107.7
|
1.0
|
OD1
|
B:ASN597
|
4.6
|
121.0
|
1.0
|
H5'1
|
B:UDP702
|
4.6
|
111.6
|
1.0
|
HB2
|
B:ASP481
|
4.6
|
115.5
|
1.0
|
HB3
|
B:ASP481
|
4.7
|
115.5
|
1.0
|
HB3
|
B:ASP479
|
4.8
|
103.0
|
1.0
|
HG3
|
B:GLU595
|
4.9
|
122.3
|
1.0
|
|
Manganese binding site 4 out
of 8 in 8vh8
Go back to
Manganese Binding Sites List in 8vh8
Manganese binding site 4 out
of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn703
b:68.2
occ:1.00
|
O3B
|
B:UDP704
|
2.1
|
69.8
|
1.0
|
OD2
|
B:ASP217
|
2.1
|
66.9
|
1.0
|
O2A
|
B:UDP704
|
2.2
|
65.8
|
1.0
|
O
|
B:HOH801
|
2.2
|
72.8
|
1.0
|
OD1
|
B:ASP217
|
2.3
|
63.4
|
1.0
|
CG
|
B:ASP217
|
2.5
|
64.0
|
1.0
|
H5'1
|
B:UDP704
|
3.1
|
73.5
|
1.0
|
PB
|
B:UDP704
|
3.2
|
69.9
|
1.0
|
PA
|
B:UDP704
|
3.3
|
66.0
|
1.0
|
O3A
|
B:UDP704
|
3.3
|
66.2
|
1.0
|
HH12
|
B:ARG247
|
3.5
|
91.1
|
1.0
|
HE
|
B:ARG320
|
3.6
|
80.7
|
1.0
|
H3'
|
B:UDP704
|
3.7
|
71.7
|
1.0
|
OD1
|
B:ASP218
|
3.8
|
68.0
|
1.0
|
OD2
|
B:ASP218
|
3.8
|
64.7
|
1.0
|
O1B
|
B:UDP704
|
3.9
|
68.8
|
1.0
|
HH21
|
B:ARG320
|
3.9
|
78.0
|
1.0
|
OD1
|
B:ASN317
|
4.0
|
76.2
|
1.0
|
C5'
|
B:UDP704
|
4.0
|
61.3
|
1.0
|
CB
|
B:ASP217
|
4.0
|
61.3
|
1.0
|
HB3
|
B:ASP215
|
4.1
|
71.5
|
1.0
|
O5'
|
B:UDP704
|
4.1
|
62.0
|
1.0
|
CG
|
B:ASP218
|
4.2
|
65.3
|
1.0
|
HB2
|
B:ASP215
|
4.2
|
71.5
|
1.0
|
HB3
|
B:ASP217
|
4.3
|
73.6
|
1.0
|
NH1
|
B:ARG247
|
4.3
|
75.9
|
1.0
|
OD2
|
B:ASP215
|
4.3
|
61.2
|
1.0
|
HB2
|
B:SER323
|
4.4
|
93.0
|
1.0
|
O
|
B:THR318
|
4.4
|
77.8
|
1.0
|
HB2
|
B:ASP217
|
4.4
|
73.6
|
1.0
|
HH22
|
B:ARG247
|
4.4
|
88.6
|
1.0
|
NE
|
B:ARG320
|
4.4
|
67.2
|
1.0
|
O2B
|
B:UDP704
|
4.5
|
71.8
|
1.0
|
O1A
|
B:UDP704
|
4.5
|
67.3
|
1.0
|
CB
|
B:ASP215
|
4.6
|
59.6
|
1.0
|
H
|
B:ASP217
|
4.6
|
70.2
|
1.0
|
H5'2
|
B:UDP704
|
4.7
|
73.5
|
1.0
|
NH2
|
B:ARG320
|
4.7
|
65.0
|
1.0
|
HH11
|
B:ARG247
|
4.7
|
91.1
|
1.0
|
C3'
|
B:UDP704
|
4.7
|
59.8
|
1.0
|
HG2
|
B:ARG320
|
4.8
|
91.5
|
1.0
|
HB
|
B:THR318
|
4.8
|
88.5
|
1.0
|
H
|
B:THR318
|
4.9
|
90.7
|
1.0
|
CG
|
B:ASP215
|
4.9
|
60.2
|
1.0
|
C4'
|
B:UDP704
|
4.9
|
59.4
|
1.0
|
|
Manganese binding site 5 out
of 8 in 8vh8
Go back to
Manganese Binding Sites List in 8vh8
Manganese binding site 5 out
of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn701
b:105.9
occ:1.00
|
O
|
C:HOH801
|
2.1
|
101.4
|
1.0
|
O2A
|
C:UDP702
|
2.2
|
105.5
|
1.0
|
OD2
|
C:ASP481
|
2.2
|
101.3
|
1.0
|
O1B
|
C:UDP702
|
2.4
|
105.1
|
1.0
|
CG
|
C:ASP481
|
3.0
|
99.4
|
1.0
|
OD1
|
C:ASP481
|
3.1
|
98.6
|
1.0
|
PA
|
C:UDP702
|
3.4
|
106.7
|
1.0
|
PB
|
C:UDP702
|
3.4
|
106.9
|
1.0
|
O3A
|
C:UDP702
|
3.5
|
106.1
|
1.0
|
HH22
|
C:ARG403
|
3.8
|
133.4
|
1.0
|
HH12
|
C:ARG403
|
3.8
|
127.8
|
1.0
|
O3B
|
C:UDP702
|
3.9
|
105.4
|
1.0
|
H5'1
|
C:UDP702
|
4.0
|
127.2
|
1.0
|
OD2
|
C:ASP479
|
4.1
|
102.0
|
1.0
|
O5'
|
C:UDP702
|
4.4
|
106.4
|
1.0
|
O1A
|
C:UDP702
|
4.4
|
106.6
|
1.0
|
CB
|
C:ASP481
|
4.4
|
98.6
|
1.0
|
NH2
|
C:ARG403
|
4.5
|
111.1
|
1.0
|
NH1
|
C:ARG403
|
4.5
|
106.5
|
1.0
|
HB3
|
C:ASP479
|
4.5
|
118.3
|
1.0
|
HB2
|
C:ASP481
|
4.7
|
118.3
|
1.0
|
O2B
|
C:UDP702
|
4.7
|
105.5
|
1.0
|
C5'
|
C:UDP702
|
4.7
|
106.0
|
1.0
|
HB3
|
C:ASP481
|
4.8
|
118.3
|
1.0
|
H3'
|
C:UDP702
|
4.9
|
125.8
|
1.0
|
HD11
|
C:ILE482
|
4.9
|
106.0
|
1.0
|
CZ
|
C:ARG403
|
4.9
|
110.1
|
1.0
|
HG13
|
C:ILE482
|
4.9
|
104.8
|
1.0
|
CG
|
C:ASP479
|
5.0
|
99.8
|
1.0
|
|
Manganese binding site 6 out
of 8 in 8vh8
Go back to
Manganese Binding Sites List in 8vh8
Manganese binding site 6 out
of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn703
b:74.5
occ:1.00
|
O
|
C:HOH802
|
2.1
|
73.7
|
1.0
|
OD2
|
C:ASP217
|
2.1
|
74.5
|
1.0
|
O3B
|
C:UDP704
|
2.1
|
75.2
|
1.0
|
OD1
|
C:ASP217
|
2.2
|
72.6
|
1.0
|
O2A
|
C:UDP704
|
2.3
|
70.4
|
1.0
|
CG
|
C:ASP217
|
2.5
|
73.5
|
1.0
|
O3A
|
C:UDP704
|
3.3
|
71.6
|
1.0
|
PB
|
C:UDP704
|
3.3
|
75.8
|
1.0
|
PA
|
C:UDP704
|
3.3
|
68.1
|
1.0
|
H5'1
|
C:UDP704
|
3.3
|
79.6
|
1.0
|
HH12
|
C:ARG247
|
3.6
|
93.4
|
1.0
|
OD1
|
C:ASP218
|
3.8
|
71.5
|
1.0
|
OD2
|
C:ASP218
|
3.8
|
69.3
|
1.0
|
H3'
|
C:UDP704
|
3.8
|
77.0
|
1.0
|
OD1
|
C:ASN317
|
3.9
|
73.4
|
1.0
|
HE
|
C:ARG320
|
3.9
|
84.1
|
1.0
|
CB
|
C:ASP217
|
4.0
|
71.1
|
1.0
|
HB3
|
C:ASP215
|
4.1
|
78.6
|
1.0
|
O1B
|
C:UDP704
|
4.1
|
76.4
|
1.0
|
CG
|
C:ASP218
|
4.2
|
70.0
|
1.0
|
HB2
|
C:ASP215
|
4.2
|
78.6
|
1.0
|
HB3
|
C:ASP217
|
4.2
|
85.3
|
1.0
|
C5'
|
C:UDP704
|
4.3
|
66.3
|
1.0
|
O5'
|
C:UDP704
|
4.3
|
66.9
|
1.0
|
NH1
|
C:ARG247
|
4.4
|
77.8
|
1.0
|
O
|
C:THR318
|
4.4
|
79.1
|
1.0
|
HB2
|
C:ASP217
|
4.4
|
85.3
|
1.0
|
O2B
|
C:UDP704
|
4.4
|
77.9
|
1.0
|
OD2
|
C:ASP215
|
4.4
|
65.3
|
1.0
|
HH21
|
C:ARG320
|
4.4
|
81.2
|
1.0
|
O1A
|
C:UDP704
|
4.5
|
72.2
|
1.0
|
H
|
C:ASP217
|
4.5
|
82.7
|
1.0
|
HH22
|
C:ARG247
|
4.6
|
94.8
|
1.0
|
CB
|
C:ASP215
|
4.6
|
65.5
|
1.0
|
H
|
C:THR318
|
4.7
|
90.1
|
1.0
|
HH11
|
C:ARG247
|
4.7
|
93.4
|
1.0
|
NE
|
C:ARG320
|
4.8
|
70.1
|
1.0
|
HB2
|
C:SER323
|
4.8
|
100.0
|
1.0
|
HB
|
C:THR318
|
4.8
|
93.1
|
1.0
|
C3'
|
C:UDP704
|
4.9
|
64.2
|
1.0
|
HG2
|
C:ARG320
|
5.0
|
92.3
|
1.0
|
CG
|
C:ASP215
|
5.0
|
64.9
|
1.0
|
CA
|
C:ASP217
|
5.0
|
69.7
|
1.0
|
H5'2
|
C:UDP704
|
5.0
|
79.6
|
1.0
|
|
Manganese binding site 7 out
of 8 in 8vh8
Go back to
Manganese Binding Sites List in 8vh8
Manganese binding site 7 out
of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 7 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn701
b:81.0
occ:1.00
|
O1B
|
D:UDP702
|
2.1
|
81.2
|
1.0
|
OD2
|
D:ASP481
|
2.2
|
76.8
|
1.0
|
O
|
D:HOH802
|
2.2
|
73.8
|
1.0
|
O2A
|
D:UDP702
|
2.4
|
80.6
|
1.0
|
CG
|
D:ASP481
|
3.1
|
75.5
|
1.0
|
OD1
|
D:ASP481
|
3.4
|
74.0
|
1.0
|
PB
|
D:UDP702
|
3.4
|
83.3
|
1.0
|
PA
|
D:UDP702
|
3.5
|
81.5
|
1.0
|
O3A
|
D:UDP702
|
3.6
|
81.3
|
1.0
|
HH22
|
D:ARG403
|
3.7
|
98.0
|
1.0
|
H5'1
|
D:UDP702
|
3.9
|
94.5
|
1.0
|
HH12
|
D:ARG403
|
4.0
|
94.1
|
1.0
|
O3B
|
D:UDP702
|
4.0
|
84.3
|
1.0
|
OD2
|
D:ASP479
|
4.4
|
70.9
|
1.0
|
NH2
|
D:ARG403
|
4.4
|
81.7
|
1.0
|
CB
|
D:ASP481
|
4.5
|
77.4
|
1.0
|
O1A
|
D:UDP702
|
4.6
|
82.5
|
1.0
|
NH1
|
D:ARG403
|
4.6
|
78.4
|
1.0
|
O2B
|
D:UDP702
|
4.6
|
83.1
|
1.0
|
O5'
|
D:UDP702
|
4.6
|
80.0
|
1.0
|
HB2
|
D:ASP481
|
4.6
|
92.9
|
1.0
|
C5'
|
D:UDP702
|
4.7
|
78.8
|
1.0
|
HB3
|
D:ASP481
|
4.7
|
92.9
|
1.0
|
HB3
|
D:ASP479
|
4.8
|
82.4
|
1.0
|
CZ
|
D:ARG403
|
4.9
|
80.5
|
1.0
|
HH21
|
D:ARG403
|
4.9
|
98.0
|
1.0
|
|
Manganese binding site 8 out
of 8 in 8vh8
Go back to
Manganese Binding Sites List in 8vh8
Manganese binding site 8 out
of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 8 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn703
b:66.1
occ:1.00
|
O
|
D:HOH801
|
2.0
|
66.0
|
1.0
|
O3B
|
D:UDP704
|
2.1
|
64.3
|
1.0
|
OD2
|
D:ASP217
|
2.1
|
63.9
|
1.0
|
OD1
|
D:ASP217
|
2.2
|
60.6
|
1.0
|
O2A
|
D:UDP704
|
2.2
|
60.1
|
1.0
|
CG
|
D:ASP217
|
2.5
|
61.9
|
1.0
|
H5'1
|
D:UDP704
|
3.0
|
69.2
|
1.0
|
O3A
|
D:UDP704
|
3.2
|
61.2
|
1.0
|
PB
|
D:UDP704
|
3.2
|
63.8
|
1.0
|
PA
|
D:UDP704
|
3.2
|
58.7
|
1.0
|
OD1
|
D:ASP218
|
3.7
|
63.3
|
1.0
|
HH12
|
D:ARG247
|
3.8
|
85.1
|
1.0
|
OD1
|
D:ASN317
|
3.8
|
71.5
|
1.0
|
H3'
|
D:UDP704
|
3.8
|
64.7
|
1.0
|
HE
|
D:ARG320
|
3.9
|
74.6
|
1.0
|
OD2
|
D:ASP218
|
3.9
|
61.3
|
1.0
|
HH21
|
D:ARG320
|
4.0
|
71.5
|
1.0
|
O1B
|
D:UDP704
|
4.0
|
63.8
|
1.0
|
C5'
|
D:UDP704
|
4.0
|
57.7
|
1.0
|
CB
|
D:ASP217
|
4.0
|
59.6
|
1.0
|
O5'
|
D:UDP704
|
4.1
|
58.1
|
1.0
|
HB3
|
D:ASP215
|
4.2
|
70.0
|
1.0
|
CG
|
D:ASP218
|
4.2
|
61.2
|
1.0
|
HB2
|
D:ASP215
|
4.2
|
70.0
|
1.0
|
HB3
|
D:ASP217
|
4.3
|
71.5
|
1.0
|
OD2
|
D:ASP215
|
4.3
|
59.9
|
1.0
|
O
|
D:THR318
|
4.4
|
72.3
|
1.0
|
O2B
|
D:UDP704
|
4.4
|
66.5
|
1.0
|
HB2
|
D:ASP217
|
4.4
|
71.5
|
1.0
|
O1A
|
D:UDP704
|
4.5
|
63.0
|
1.0
|
HB2
|
D:SER323
|
4.5
|
83.7
|
1.0
|
NH1
|
D:ARG247
|
4.5
|
71.0
|
1.0
|
CB
|
D:ASP215
|
4.6
|
58.3
|
1.0
|
H5'2
|
D:UDP704
|
4.6
|
69.2
|
1.0
|
H
|
D:ASP217
|
4.7
|
66.8
|
1.0
|
NE
|
D:ARG320
|
4.7
|
62.2
|
1.0
|
NH2
|
D:ARG320
|
4.8
|
59.6
|
1.0
|
HH22
|
D:ARG247
|
4.8
|
82.3
|
1.0
|
C3'
|
D:UDP704
|
4.8
|
54.0
|
1.0
|
HH11
|
D:ARG247
|
4.8
|
85.1
|
1.0
|
H
|
D:THR318
|
4.9
|
83.8
|
1.0
|
CG
|
D:ASP215
|
4.9
|
58.8
|
1.0
|
HB
|
D:THR318
|
4.9
|
81.6
|
1.0
|
C4'
|
D:UDP704
|
5.0
|
55.1
|
1.0
|
CG
|
D:ASN317
|
5.0
|
72.2
|
1.0
|
|
Reference:
E.Stancanelli,
J.A.Krahn,
E.Viverette,
R.Dutcher,
V.Pagadala,
M.J.Borgnia,
J.Liu,
L.C.Pedersen.
Structural and Functional Analysis of Heparosan Synthase 2 From Pasteurella Multocida to Improve the Synthesis of Heparin Acs Catalysis V. 14 6577 2024.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.4C00677
Page generated: Sun Oct 6 14:04:21 2024
|