Zinc in PDB 5l9e: Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
Enzymatic activity of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
All present enzymatic activity of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer:
4.2.1.1;
Protein crystallography data
The structure of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer, PDB code: 5l9e
was solved by
M.Vallade,
B.Langlois D'estaintot,
T.Granier,
I.Huc,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
85.39 /
2.90
|
Space group
|
I 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
125.972,
75.140,
141.098,
90.00,
100.08,
90.00
|
R / Rfree (%)
|
24.2 /
27.3
|
Zinc Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
27;
Binding sites:
The binding sites of Zinc atom in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
(pdb code 5l9e). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 27 binding sites of Zinc where determined in the
Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer, PDB code: 5l9e:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Zinc binding site 1 out
of 27 in 5l9e
Go back to
Zinc Binding Sites List in 5l9e
Zinc binding site 1 out
of 27 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:45.5
occ:1.00
|
NE2
|
A:HIS94
|
2.0
|
45.5
|
1.0
|
NE2
|
A:HIS96
|
2.0
|
46.1
|
1.0
|
N26
|
A:6H0302
|
2.1
|
45.8
|
1.0
|
ND1
|
A:HIS119
|
2.2
|
45.5
|
1.0
|
O25
|
A:6H0302
|
2.7
|
45.2
|
1.0
|
S24
|
A:6H0302
|
2.9
|
45.6
|
1.0
|
CE1
|
A:HIS96
|
2.9
|
46.7
|
1.0
|
CE1
|
A:HIS94
|
2.9
|
45.5
|
1.0
|
CD2
|
A:HIS94
|
3.0
|
45.9
|
1.0
|
CD2
|
A:HIS96
|
3.0
|
46.5
|
1.0
|
CE1
|
A:HIS119
|
3.1
|
45.9
|
1.0
|
CG
|
A:HIS119
|
3.3
|
45.5
|
1.0
|
CB
|
A:HIS119
|
3.7
|
45.3
|
1.0
|
OG1
|
A:THR198
|
3.8
|
46.7
|
1.0
|
C21
|
A:6H0302
|
4.0
|
46.0
|
1.0
|
O27
|
A:6H0302
|
4.0
|
45.9
|
1.0
|
ND1
|
A:HIS94
|
4.1
|
45.9
|
1.0
|
ND1
|
A:HIS96
|
4.1
|
47.3
|
1.0
|
CG
|
A:HIS94
|
4.1
|
46.1
|
1.0
|
CG
|
A:HIS96
|
4.1
|
47.2
|
1.0
|
OE1
|
A:GLU106
|
4.2
|
47.0
|
1.0
|
NE2
|
A:HIS119
|
4.3
|
46.2
|
1.0
|
CD2
|
A:HIS119
|
4.4
|
45.9
|
1.0
|
C20
|
A:6H0302
|
4.7
|
46.5
|
1.0
|
C22
|
A:6H0302
|
4.8
|
46.0
|
1.0
|
CD
|
A:GLU106
|
4.9
|
47.7
|
1.0
|
|
Zinc binding site 2 out
of 27 in 5l9e
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Zinc Binding Sites List in 5l9e
Zinc binding site 2 out
of 27 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn307
b:57.5
occ:1.00
|
NE2
|
A:HIS64
|
2.0
|
55.1
|
1.0
|
NE2
|
A:HIS4
|
2.1
|
59.8
|
1.0
|
CE1
|
A:HIS64
|
3.0
|
55.3
|
1.0
|
CE1
|
A:HIS4
|
3.0
|
61.4
|
1.0
|
CD2
|
A:HIS64
|
3.0
|
53.6
|
1.0
|
CD2
|
A:HIS4
|
3.1
|
60.7
|
1.0
|
ND1
|
A:HIS64
|
4.1
|
54.0
|
1.0
|
CG
|
A:HIS64
|
4.2
|
52.8
|
1.0
|
ND1
|
A:HIS4
|
4.2
|
63.3
|
1.0
|
CG
|
A:HIS4
|
4.2
|
62.9
|
1.0
|
NE1
|
A:TRP5
|
4.3
|
55.4
|
1.0
|
O
|
A:ASN62
|
4.5
|
55.8
|
1.0
|
CE2
|
A:TRP5
|
4.7
|
54.0
|
1.0
|
CZ2
|
A:TRP5
|
4.8
|
52.5
|
1.0
|
|
Zinc binding site 3 out
of 27 in 5l9e
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Zinc Binding Sites List in 5l9e
Zinc binding site 3 out
of 27 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn308
b:76.5
occ:1.00
|
NE2
|
A:HIS17
|
2.0
|
72.3
|
1.0
|
CE1
|
A:HIS17
|
2.8
|
70.1
|
1.0
|
CD2
|
A:HIS17
|
3.1
|
71.2
|
1.0
|
ND1
|
A:HIS17
|
4.0
|
67.6
|
1.0
|
CG
|
A:HIS17
|
4.1
|
68.2
|
1.0
|
CG
|
A:LYS18
|
4.5
|
73.2
|
1.0
|
CD
|
A:LYS18
|
4.9
|
73.9
|
1.0
|
|
Zinc binding site 4 out
of 27 in 5l9e
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Zinc Binding Sites List in 5l9e
Zinc binding site 4 out
of 27 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn309
b:77.5
occ:0.50
|
OD2
|
A:ASP174
|
2.0
|
75.2
|
1.0
|
OD1
|
A:ASP174
|
2.0
|
72.5
|
1.0
|
CG
|
A:ASP174
|
2.2
|
73.0
|
1.0
|
O
|
C:HOH428
|
2.5
|
0.2
|
1.0
|
O
|
A:HOH443
|
2.8
|
0.2
|
1.0
|
CB
|
A:ASP174
|
3.5
|
71.1
|
1.0
|
CB
|
C:ASP161
|
4.5
|
69.5
|
1.0
|
O
|
A:HOH428
|
4.5
|
0.2
|
1.0
|
O
|
C:ASP161
|
4.5
|
68.2
|
1.0
|
CA
|
A:ASP174
|
4.7
|
67.8
|
1.0
|
O
|
A:HOH420
|
4.8
|
0.2
|
1.0
|
OD2
|
C:ASP161
|
4.8
|
73.6
|
1.0
|
CG
|
C:ASP161
|
4.8
|
71.4
|
1.0
|
|
Zinc binding site 5 out
of 27 in 5l9e
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Zinc Binding Sites List in 5l9e
Zinc binding site 5 out
of 27 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn310
b:80.4
occ:1.00
|
O
|
A:HOH401
|
2.0
|
0.2
|
1.0
|
OD1
|
A:ASP34
|
2.0
|
75.1
|
1.0
|
ND1
|
A:HIS36
|
2.3
|
82.1
|
1.0
|
CG
|
A:ASP34
|
2.7
|
73.8
|
1.0
|
OD2
|
A:ASP34
|
2.7
|
75.6
|
1.0
|
CG
|
A:HIS36
|
3.2
|
83.6
|
1.0
|
CE1
|
A:HIS36
|
3.2
|
83.6
|
1.0
|
CB
|
A:HIS36
|
3.5
|
82.8
|
1.0
|
CB
|
A:ASP34
|
4.2
|
70.3
|
1.0
|
NE2
|
A:HIS36
|
4.3
|
85.9
|
1.0
|
N
|
A:HIS36
|
4.3
|
76.7
|
1.0
|
CD2
|
A:HIS36
|
4.3
|
86.0
|
1.0
|
OD1
|
A:ASP110
|
4.5
|
72.0
|
1.0
|
CA
|
A:HIS36
|
4.5
|
80.1
|
1.0
|
CA
|
A:ASP34
|
5.0
|
68.2
|
1.0
|
|
Zinc binding site 6 out
of 27 in 5l9e
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Zinc Binding Sites List in 5l9e
Zinc binding site 6 out
of 27 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn311
b:78.7
occ:1.00
|
OE2
|
A:GLU186
|
2.0
|
73.7
|
1.0
|
O
|
A:HOH433
|
2.0
|
0.2
|
1.0
|
O
|
A:HOH404
|
2.0
|
0.2
|
1.0
|
OD2
|
B:ASP189
|
2.0
|
70.3
|
1.0
|
OE1
|
A:GLU186
|
2.0
|
76.1
|
1.0
|
OD1
|
B:ASP189
|
2.0
|
69.3
|
1.0
|
CD
|
A:GLU186
|
2.2
|
73.7
|
1.0
|
CG
|
B:ASP189
|
2.3
|
68.5
|
1.0
|
CG
|
A:GLU186
|
3.7
|
71.2
|
1.0
|
CB
|
B:ASP189
|
3.9
|
65.6
|
1.0
|
OG
|
B:SER187
|
4.3
|
66.5
|
1.0
|
CB
|
B:PHE259
|
4.6
|
71.9
|
1.0
|
CA
|
B:ASP189
|
4.7
|
63.5
|
1.0
|
CB
|
A:GLU186
|
4.8
|
69.2
|
1.0
|
|
Zinc binding site 7 out
of 27 in 5l9e
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Zinc Binding Sites List in 5l9e
Zinc binding site 7 out
of 27 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn312
b:66.6
occ:1.00
|
O
|
A:HOH425
|
2.0
|
0.2
|
1.0
|
O
|
B:HOH418
|
2.0
|
0.2
|
1.0
|
OD1
|
B:ASP52
|
2.0
|
67.2
|
1.0
|
OD2
|
B:ASP52
|
2.0
|
71.0
|
1.0
|
OD2
|
A:ASP52
|
2.0
|
69.7
|
1.0
|
OD1
|
A:ASP52
|
2.1
|
66.1
|
1.0
|
CG
|
B:ASP52
|
2.2
|
69.0
|
1.0
|
CG
|
A:ASP52
|
2.3
|
67.9
|
1.0
|
CB
|
B:ASP52
|
3.6
|
69.2
|
1.0
|
CB
|
A:ASP52
|
3.6
|
68.0
|
1.0
|
N
|
A:ASP52
|
4.0
|
63.1
|
1.0
|
N
|
B:ASP52
|
4.1
|
64.2
|
1.0
|
CA
|
B:ASP52
|
4.3
|
66.6
|
1.0
|
CA
|
A:ASP52
|
4.3
|
65.4
|
1.0
|
O
|
A:VAL49
|
4.4
|
60.3
|
1.0
|
N
|
A:TYR51
|
4.4
|
59.6
|
1.0
|
CD
|
B:ARG181
|
4.4
|
63.2
|
1.0
|
O
|
B:VAL49
|
4.5
|
61.5
|
1.0
|
N
|
B:TYR51
|
4.5
|
60.8
|
1.0
|
CD
|
A:ARG181
|
4.5
|
62.4
|
1.0
|
NH1
|
B:ARG181
|
4.5
|
68.9
|
1.0
|
CA
|
A:SER50
|
4.6
|
60.8
|
1.0
|
NH1
|
A:ARG181
|
4.7
|
67.9
|
1.0
|
CA
|
B:SER50
|
4.8
|
62.2
|
1.0
|
NE
|
B:ARG181
|
4.9
|
64.5
|
1.0
|
C
|
A:TYR51
|
4.9
|
60.9
|
1.0
|
C
|
A:SER50
|
4.9
|
59.8
|
1.0
|
C
|
B:TYR51
|
5.0
|
62.0
|
1.0
|
CZ
|
B:ARG181
|
5.0
|
67.2
|
1.0
|
|
Zinc binding site 8 out
of 27 in 5l9e
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Zinc Binding Sites List in 5l9e
Zinc binding site 8 out
of 27 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn313
b:73.7
occ:0.50
|
O
|
A:HOH427
|
3.1
|
0.2
|
1.0
|
NE2
|
A:HIS15
|
3.4
|
71.2
|
1.0
|
CE1
|
A:HIS15
|
3.9
|
73.0
|
1.0
|
CG
|
A:GLU14
|
4.0
|
68.2
|
1.0
|
O
|
A:LYS9
|
4.4
|
71.0
|
1.0
|
CB
|
A:GLU14
|
4.4
|
65.5
|
1.0
|
CD2
|
A:HIS15
|
4.4
|
68.7
|
1.0
|
|
Zinc binding site 9 out
of 27 in 5l9e
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Zinc Binding Sites List in 5l9e
Zinc binding site 9 out
of 27 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 9 of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn315
b:78.0
occ:1.00
|
OE2
|
B:GLU186
|
2.0
|
73.2
|
1.0
|
OE1
|
B:GLU186
|
2.0
|
75.3
|
1.0
|
OD2
|
A:ASP189
|
2.0
|
70.2
|
1.0
|
OD1
|
A:ASP189
|
2.1
|
68.6
|
1.0
|
CD
|
B:GLU186
|
2.3
|
73.1
|
1.0
|
CG
|
A:ASP189
|
2.4
|
68.0
|
1.0
|
O
|
A:HOH441
|
3.2
|
0.2
|
1.0
|
NZ
|
A:LYS260
|
3.4
|
79.5
|
1.0
|
CG
|
B:GLU186
|
3.8
|
70.7
|
1.0
|
CE
|
A:LYS260
|
3.9
|
78.3
|
1.0
|
CB
|
A:ASP189
|
3.9
|
65.1
|
1.0
|
OG
|
A:SER187
|
4.3
|
66.4
|
1.0
|
CB
|
A:PHE259
|
4.6
|
70.8
|
1.0
|
CA
|
A:ASP189
|
4.8
|
62.8
|
1.0
|
CD
|
A:LYS260
|
4.8
|
81.1
|
1.0
|
CB
|
B:GLU186
|
4.9
|
68.8
|
1.0
|
|
Zinc binding site 10 out
of 27 in 5l9e
Go back to
Zinc Binding Sites List in 5l9e
Zinc binding site 10 out
of 27 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 10 of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn316
b:0.2
occ:0.50
|
OE2
|
A:GLU233
|
2.0
|
86.3
|
1.0
|
OE2
|
C:GLU233
|
2.0
|
81.3
|
1.0
|
OE1
|
C:GLU233
|
2.4
|
76.1
|
1.0
|
CD
|
C:GLU233
|
2.5
|
78.4
|
1.0
|
CD
|
A:GLU233
|
2.8
|
82.9
|
1.0
|
OE1
|
A:GLU233
|
3.0
|
80.4
|
1.0
|
NZ
|
C:LYS171
|
3.8
|
72.9
|
1.0
|
CG
|
C:GLU233
|
4.0
|
77.8
|
1.0
|
NZ
|
A:LYS171
|
4.1
|
76.7
|
1.0
|
CG
|
A:GLU233
|
4.2
|
82.1
|
1.0
|
CB
|
C:GLU233
|
4.9
|
75.4
|
1.0
|
|
Reference:
M.Vallade,
L.Fischer,
B.Langlois D'estaintot,
T.Granier,
I.Huc.
Crystal Structure of Human Carbonic Anhydrase II in Complex with A Quinoline Oligoamide Foldamer To Be Published.
Page generated: Wed Dec 16 06:28:29 2020
|