Zinc in PDB 6ica: The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase
Protein crystallography data
The structure of The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase, PDB code: 6ica
was solved by
G.Honghua,
Z.Nannan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
34.52 /
2.20
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
84.424,
121.913,
130.812,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
14.3 /
18.3
|
Zinc Binding Sites:
The binding sites of Zinc atom in the The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase
(pdb code 6ica). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase, PDB code: 6ica:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 6ica
Go back to
Zinc Binding Sites List in 6ica
Zinc binding site 1 out
of 6 in the The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn504
b:19.4
occ:1.00
|
O
|
A:HOH653
|
1.9
|
16.5
|
1.0
|
OD1
|
A:ASP251
|
2.1
|
19.6
|
1.0
|
NE2
|
A:HIS238
|
2.1
|
18.1
|
1.0
|
OD1
|
A:ASP313
|
2.2
|
14.8
|
1.0
|
OD2
|
A:ASP313
|
2.4
|
18.4
|
1.0
|
O
|
A:HOH784
|
2.4
|
25.7
|
1.0
|
CG
|
A:ASP313
|
2.6
|
19.6
|
1.0
|
CG
|
A:ASP251
|
3.0
|
20.8
|
1.0
|
CE1
|
A:HIS238
|
3.1
|
14.4
|
1.0
|
CD2
|
A:HIS238
|
3.2
|
13.4
|
1.0
|
ZN
|
A:ZN505
|
3.3
|
55.1
|
1.0
|
OD2
|
A:ASP251
|
3.3
|
29.9
|
1.0
|
OE1
|
A:GLU285
|
3.9
|
26.3
|
1.0
|
OE2
|
A:GLU286
|
3.9
|
27.4
|
1.0
|
CB
|
A:ASP252
|
4.0
|
13.7
|
1.0
|
CB
|
A:ASP313
|
4.1
|
19.5
|
1.0
|
ND1
|
A:HIS238
|
4.2
|
13.1
|
1.0
|
CD
|
A:GLU285
|
4.3
|
29.6
|
1.0
|
CB
|
A:ASP251
|
4.3
|
15.4
|
1.0
|
CG
|
A:HIS238
|
4.3
|
13.7
|
1.0
|
OE2
|
A:GLU285
|
4.4
|
38.6
|
1.0
|
CG
|
A:MET314
|
4.6
|
11.0
|
1.0
|
CA
|
A:ASP251
|
4.7
|
12.6
|
1.0
|
CG
|
A:ASP252
|
4.7
|
17.9
|
1.0
|
C
|
A:ASP251
|
4.8
|
14.1
|
1.0
|
CD
|
A:GLU286
|
4.8
|
24.7
|
1.0
|
CA
|
A:ASP313
|
4.8
|
14.3
|
1.0
|
N
|
A:ASP252
|
4.9
|
12.1
|
1.0
|
OG
|
A:SER363
|
4.9
|
12.2
|
1.0
|
CA
|
A:ASP252
|
4.9
|
15.3
|
1.0
|
|
Zinc binding site 2 out
of 6 in 6ica
Go back to
Zinc Binding Sites List in 6ica
Zinc binding site 2 out
of 6 in the The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn505
b:55.1
occ:1.00
|
OD2
|
A:ASP251
|
2.2
|
29.9
|
1.0
|
O
|
A:HOH653
|
2.2
|
16.5
|
1.0
|
NE2
|
A:HIS391
|
2.2
|
20.0
|
1.0
|
OE2
|
A:GLU286
|
2.2
|
27.4
|
1.0
|
OE1
|
A:GLU286
|
2.9
|
23.8
|
1.0
|
CD
|
A:GLU286
|
2.9
|
24.7
|
1.0
|
CG
|
A:ASP251
|
3.1
|
20.8
|
1.0
|
CE1
|
A:HIS391
|
3.1
|
20.0
|
1.0
|
CD2
|
A:HIS391
|
3.2
|
20.6
|
1.0
|
O
|
A:HOH669
|
3.3
|
39.1
|
1.0
|
ZN
|
A:ZN504
|
3.3
|
19.4
|
1.0
|
OD1
|
A:ASP251
|
3.4
|
19.6
|
1.0
|
O
|
A:HOH784
|
3.4
|
25.7
|
1.0
|
OE1
|
A:GLU285
|
4.1
|
26.3
|
1.0
|
O
|
A:HOH624
|
4.1
|
23.5
|
1.0
|
ND1
|
A:HIS391
|
4.3
|
19.6
|
1.0
|
CG
|
A:HIS391
|
4.3
|
21.3
|
1.0
|
CG
|
A:GLU286
|
4.4
|
19.8
|
1.0
|
CB
|
A:ASP251
|
4.4
|
15.4
|
1.0
|
NE2
|
A:HIS238
|
4.5
|
18.1
|
1.0
|
CE1
|
A:HIS238
|
4.6
|
14.4
|
1.0
|
CD
|
A:GLU285
|
4.9
|
29.6
|
1.0
|
|
Zinc binding site 3 out
of 6 in 6ica
Go back to
Zinc Binding Sites List in 6ica
Zinc binding site 3 out
of 6 in the The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn504
b:20.0
occ:1.00
|
OD1
|
B:ASP251
|
2.0
|
16.2
|
1.0
|
NE2
|
B:HIS238
|
2.2
|
17.7
|
1.0
|
OD1
|
B:ASP313
|
2.2
|
16.6
|
1.0
|
O
|
B:HOH745
|
2.3
|
34.2
|
1.0
|
OD2
|
B:ASP313
|
2.3
|
18.4
|
1.0
|
CG
|
B:ASP313
|
2.6
|
18.1
|
1.0
|
CG
|
B:ASP251
|
3.0
|
22.1
|
1.0
|
CE1
|
B:HIS238
|
3.1
|
10.5
|
1.0
|
CD2
|
B:HIS238
|
3.1
|
10.9
|
1.0
|
ZN
|
B:ZN505
|
3.2
|
54.8
|
1.0
|
OD2
|
B:ASP251
|
3.5
|
32.3
|
1.0
|
OE1
|
B:GLU285
|
3.8
|
23.1
|
1.0
|
CB
|
B:ASP252
|
4.1
|
17.4
|
1.0
|
OE2
|
B:GLU286
|
4.1
|
31.4
|
1.0
|
CB
|
B:ASP313
|
4.1
|
15.1
|
1.0
|
CD
|
B:GLU285
|
4.2
|
24.1
|
1.0
|
ND1
|
B:HIS238
|
4.2
|
14.4
|
1.0
|
CG
|
B:HIS238
|
4.3
|
13.4
|
1.0
|
OE2
|
B:GLU285
|
4.3
|
30.9
|
1.0
|
CB
|
B:ASP251
|
4.3
|
16.4
|
1.0
|
CG
|
B:MET314
|
4.6
|
14.4
|
1.0
|
CA
|
B:ASP251
|
4.7
|
13.9
|
1.0
|
CG
|
B:ASP252
|
4.7
|
21.7
|
1.0
|
C
|
B:ASP251
|
4.8
|
14.7
|
1.0
|
CD
|
B:GLU286
|
4.9
|
28.3
|
1.0
|
N
|
B:ASP252
|
4.9
|
13.1
|
1.0
|
CA
|
B:ASP313
|
4.9
|
15.3
|
1.0
|
OG
|
B:SER363
|
4.9
|
16.7
|
1.0
|
CA
|
B:ASP252
|
4.9
|
12.5
|
1.0
|
SD
|
B:MET314
|
5.0
|
24.1
|
1.0
|
|
Zinc binding site 4 out
of 6 in 6ica
Go back to
Zinc Binding Sites List in 6ica
Zinc binding site 4 out
of 6 in the The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn505
b:54.8
occ:1.00
|
OD2
|
B:ASP251
|
2.3
|
32.3
|
1.0
|
OE2
|
B:GLU286
|
2.4
|
31.4
|
1.0
|
NE2
|
B:HIS391
|
2.5
|
28.9
|
1.0
|
OE1
|
B:GLU286
|
2.8
|
29.9
|
1.0
|
CD
|
B:GLU286
|
3.0
|
28.3
|
1.0
|
CG
|
B:ASP251
|
3.1
|
22.1
|
1.0
|
ZN
|
B:ZN504
|
3.2
|
20.0
|
1.0
|
OD1
|
B:ASP251
|
3.2
|
16.2
|
1.0
|
O
|
B:HOH745
|
3.3
|
34.2
|
1.0
|
CE1
|
B:HIS391
|
3.4
|
28.4
|
1.0
|
CD2
|
B:HIS391
|
3.5
|
25.7
|
1.0
|
OE1
|
B:GLU285
|
3.9
|
23.1
|
1.0
|
O
|
B:HOH640
|
4.4
|
19.5
|
1.0
|
NE2
|
B:HIS238
|
4.4
|
17.7
|
1.0
|
CG
|
B:GLU286
|
4.4
|
21.4
|
1.0
|
ND1
|
B:HIS391
|
4.5
|
31.5
|
1.0
|
CE1
|
B:HIS238
|
4.5
|
10.5
|
1.0
|
CB
|
B:ASP251
|
4.5
|
16.4
|
1.0
|
CG
|
B:HIS391
|
4.6
|
26.8
|
1.0
|
CD
|
B:GLU285
|
4.7
|
24.1
|
1.0
|
OE2
|
B:GLU285
|
4.8
|
30.9
|
1.0
|
CG2
|
B:ILE390
|
4.9
|
34.5
|
1.0
|
|
Zinc binding site 5 out
of 6 in 6ica
Go back to
Zinc Binding Sites List in 6ica
Zinc binding site 5 out
of 6 in the The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn504
b:19.8
occ:1.00
|
OD1
|
C:ASP251
|
2.0
|
15.0
|
1.0
|
O
|
C:HOH688
|
2.2
|
32.0
|
1.0
|
NE2
|
C:HIS238
|
2.2
|
15.8
|
1.0
|
OD1
|
C:ASP313
|
2.2
|
16.5
|
1.0
|
OD2
|
C:ASP313
|
2.4
|
17.7
|
1.0
|
O
|
C:HOH783
|
2.6
|
28.1
|
1.0
|
CG
|
C:ASP313
|
2.6
|
19.1
|
1.0
|
CG
|
C:ASP251
|
3.0
|
16.8
|
1.0
|
CE1
|
C:HIS238
|
3.1
|
9.5
|
1.0
|
CD2
|
C:HIS238
|
3.2
|
10.1
|
1.0
|
ZN
|
C:ZN505
|
3.3
|
53.4
|
1.0
|
OD2
|
C:ASP251
|
3.4
|
24.1
|
1.0
|
OE2
|
C:GLU285
|
3.9
|
21.9
|
1.0
|
OE2
|
C:GLU286
|
4.0
|
36.2
|
1.0
|
CB
|
C:ASP252
|
4.0
|
13.7
|
1.0
|
CB
|
C:ASP313
|
4.2
|
12.7
|
1.0
|
ND1
|
C:HIS238
|
4.2
|
16.3
|
1.0
|
CD
|
C:GLU285
|
4.3
|
28.6
|
1.0
|
CB
|
C:ASP251
|
4.3
|
18.1
|
1.0
|
O
|
C:HOH806
|
4.3
|
43.5
|
1.0
|
CG
|
C:HIS238
|
4.3
|
13.1
|
1.0
|
OE1
|
C:GLU285
|
4.4
|
33.0
|
1.0
|
CG
|
C:MET314
|
4.6
|
15.9
|
1.0
|
CA
|
C:ASP251
|
4.7
|
20.2
|
1.0
|
CG
|
C:ASP252
|
4.7
|
16.7
|
1.0
|
C
|
C:ASP251
|
4.8
|
16.4
|
1.0
|
CD
|
C:GLU286
|
4.9
|
33.6
|
1.0
|
N
|
C:ASP252
|
4.9
|
13.4
|
1.0
|
OG
|
C:SER363
|
4.9
|
20.2
|
1.0
|
CA
|
C:ASP252
|
4.9
|
14.7
|
1.0
|
CA
|
C:ASP313
|
4.9
|
13.8
|
1.0
|
SD
|
C:MET314
|
5.0
|
24.2
|
1.0
|
OD2
|
C:ASP252
|
5.0
|
13.8
|
1.0
|
|
Zinc binding site 6 out
of 6 in 6ica
Go back to
Zinc Binding Sites List in 6ica
Zinc binding site 6 out
of 6 in the The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn505
b:53.4
occ:1.00
|
OD2
|
C:ASP251
|
2.1
|
24.1
|
1.0
|
O
|
C:HOH688
|
2.2
|
32.0
|
1.0
|
NE2
|
C:HIS391
|
2.3
|
30.1
|
1.0
|
OE2
|
C:GLU286
|
2.4
|
36.2
|
1.0
|
OE1
|
C:GLU286
|
2.8
|
32.5
|
1.0
|
CD
|
C:GLU286
|
3.0
|
33.6
|
1.0
|
CG
|
C:ASP251
|
3.1
|
16.8
|
1.0
|
O
|
C:HOH806
|
3.1
|
43.5
|
1.0
|
CE1
|
C:HIS391
|
3.2
|
21.1
|
1.0
|
O
|
C:HOH783
|
3.3
|
28.1
|
1.0
|
ZN
|
C:ZN504
|
3.3
|
19.8
|
1.0
|
CD2
|
C:HIS391
|
3.3
|
27.8
|
1.0
|
OD1
|
C:ASP251
|
3.3
|
15.0
|
1.0
|
OE2
|
C:GLU285
|
4.0
|
21.9
|
1.0
|
O
|
C:HOH628
|
4.3
|
21.6
|
1.0
|
ND1
|
C:HIS391
|
4.3
|
27.6
|
1.0
|
CG
|
C:HIS391
|
4.4
|
27.8
|
1.0
|
CB
|
C:ASP251
|
4.4
|
18.1
|
1.0
|
CG
|
C:GLU286
|
4.5
|
30.1
|
1.0
|
NE2
|
C:HIS238
|
4.6
|
15.8
|
1.0
|
CG2
|
C:ILE390
|
4.6
|
41.5
|
1.0
|
CE1
|
C:HIS238
|
4.6
|
9.5
|
1.0
|
CD
|
C:GLU285
|
4.9
|
28.6
|
1.0
|
OE1
|
C:GLU285
|
5.0
|
33.0
|
1.0
|
|
Reference:
G.Honghua,
Z.Nannan.
The Crystal Structure of Legionella Pneumophila Lapa Aminopeptidase To Be Published.
Page generated: Mon Oct 28 23:42:08 2024
|