Zinc in PDB 2ek9: Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin
Protein crystallography data
The structure of Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin, PDB code: 2ek9
was solved by
M.Akioka,
H.Nakano,
K.Watanabe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
15.00 /
1.97
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
93.813,
68.678,
77.044,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.9 /
21.9
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin
(pdb code 2ek9). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin, PDB code: 2ek9:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 2ek9
Go back to
Zinc Binding Sites List in 2ek9
Zinc binding site 1 out
of 6 in the Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1001
b:19.5
occ:1.00
|
OD2
|
A:ASP240
|
2.1
|
13.4
|
1.0
|
O2
|
A:BES2001
|
2.1
|
24.2
|
1.0
|
OE2
|
A:GLU273
|
2.2
|
18.5
|
1.0
|
O3
|
A:BES2001
|
2.2
|
25.8
|
1.0
|
NE2
|
A:HIS371
|
2.2
|
19.6
|
1.0
|
OE1
|
A:GLU273
|
2.4
|
19.1
|
1.0
|
CD
|
A:GLU273
|
2.6
|
17.3
|
1.0
|
C3
|
A:BES2001
|
2.9
|
27.8
|
1.0
|
C2
|
A:BES2001
|
3.0
|
27.2
|
1.0
|
CG
|
A:ASP240
|
3.1
|
14.7
|
1.0
|
CD2
|
A:HIS371
|
3.2
|
19.1
|
1.0
|
CE1
|
A:HIS371
|
3.2
|
21.3
|
1.0
|
OD1
|
A:ASP240
|
3.3
|
14.1
|
1.0
|
ZN
|
A:ZN1002
|
3.5
|
17.4
|
1.0
|
N2
|
A:BES2001
|
3.6
|
26.9
|
1.0
|
CE1
|
A:TYR370
|
3.8
|
28.1
|
1.0
|
C1
|
A:BES2001
|
3.9
|
28.0
|
1.0
|
O
|
A:HOH3072
|
3.9
|
12.4
|
1.0
|
CG
|
A:GLU273
|
4.1
|
15.1
|
1.0
|
N1
|
A:BES2001
|
4.2
|
27.7
|
1.0
|
OE1
|
A:GLU272
|
4.2
|
14.9
|
1.0
|
ND1
|
A:HIS371
|
4.3
|
18.3
|
1.0
|
CG
|
A:HIS371
|
4.3
|
20.1
|
1.0
|
OH
|
A:TYR370
|
4.3
|
29.3
|
1.0
|
CB
|
A:ASP240
|
4.4
|
13.7
|
1.0
|
NE2
|
A:HIS228
|
4.5
|
14.5
|
1.0
|
CZ
|
A:TYR370
|
4.5
|
27.4
|
1.0
|
CG1
|
A:VAL232
|
4.6
|
16.9
|
1.0
|
CE1
|
A:HIS228
|
4.6
|
11.3
|
1.0
|
CD1
|
A:TYR370
|
4.7
|
25.5
|
1.0
|
O
|
A:HOH3120
|
4.7
|
29.0
|
1.0
|
C6
|
A:BES2001
|
4.8
|
31.4
|
1.0
|
C4
|
A:BES2001
|
4.9
|
29.7
|
1.0
|
|
Zinc binding site 2 out
of 6 in 2ek9
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Zinc Binding Sites List in 2ek9
Zinc binding site 2 out
of 6 in the Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1002
b:17.4
occ:1.00
|
O2
|
A:BES2001
|
1.7
|
24.2
|
1.0
|
OD1
|
A:ASP240
|
2.0
|
14.1
|
1.0
|
OD1
|
A:ASP301
|
2.2
|
12.7
|
1.0
|
NE2
|
A:HIS228
|
2.2
|
14.5
|
1.0
|
OD2
|
A:ASP301
|
2.3
|
13.2
|
1.0
|
CG
|
A:ASP301
|
2.6
|
12.1
|
1.0
|
C2
|
A:BES2001
|
2.7
|
27.2
|
1.0
|
CG
|
A:ASP240
|
3.0
|
14.7
|
1.0
|
N2
|
A:BES2001
|
3.1
|
26.9
|
1.0
|
C1
|
A:BES2001
|
3.1
|
28.0
|
1.0
|
CD2
|
A:HIS228
|
3.2
|
11.6
|
1.0
|
CE1
|
A:HIS228
|
3.3
|
11.3
|
1.0
|
OD2
|
A:ASP240
|
3.4
|
13.4
|
1.0
|
ZN
|
A:ZN1001
|
3.5
|
19.5
|
1.0
|
OE1
|
A:GLU272
|
3.9
|
14.9
|
1.0
|
C3
|
A:BES2001
|
4.0
|
27.8
|
1.0
|
OE2
|
A:GLU273
|
4.0
|
18.5
|
1.0
|
CB
|
A:ASP241
|
4.1
|
12.4
|
1.0
|
CB
|
A:ASP301
|
4.1
|
12.3
|
1.0
|
OE2
|
A:GLU272
|
4.2
|
15.4
|
1.0
|
CD
|
A:GLU272
|
4.2
|
15.3
|
1.0
|
CB
|
A:ASP240
|
4.3
|
13.7
|
1.0
|
CG
|
A:HIS228
|
4.3
|
13.6
|
1.0
|
ND1
|
A:HIS228
|
4.3
|
14.3
|
1.0
|
O3
|
A:BES2001
|
4.4
|
25.8
|
1.0
|
CG
|
A:ASP241
|
4.6
|
12.6
|
1.0
|
CA
|
A:ASP240
|
4.6
|
13.3
|
1.0
|
SD
|
A:MET302
|
4.6
|
16.5
|
1.0
|
C6
|
A:BES2001
|
4.6
|
31.4
|
1.0
|
CG
|
A:MET302
|
4.7
|
13.0
|
1.0
|
CD
|
A:GLU273
|
4.8
|
17.3
|
1.0
|
OD2
|
A:ASP241
|
4.8
|
11.4
|
1.0
|
C
|
A:ASP240
|
4.9
|
12.8
|
1.0
|
CA
|
A:ASP301
|
4.9
|
11.6
|
1.0
|
OG
|
A:SER346
|
5.0
|
14.5
|
1.0
|
|
Zinc binding site 3 out
of 6 in 2ek9
Go back to
Zinc Binding Sites List in 2ek9
Zinc binding site 3 out
of 6 in the Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1003
b:21.2
occ:1.00
|
OD2
|
A:ASP390
|
2.0
|
15.5
|
1.0
|
OD2
|
A:ASP386
|
2.0
|
16.2
|
1.0
|
O
|
A:HOH3247
|
2.1
|
17.5
|
1.0
|
CG
|
A:ASP390
|
2.8
|
13.5
|
1.0
|
CG
|
A:ASP386
|
2.9
|
15.4
|
1.0
|
OD1
|
A:ASP390
|
3.0
|
14.5
|
1.0
|
OD1
|
A:ASP386
|
3.2
|
13.9
|
1.0
|
ZN
|
A:ZN1004
|
3.3
|
19.7
|
1.0
|
O
|
A:HOH3163
|
3.6
|
20.7
|
1.0
|
O
|
A:HOH3170
|
3.7
|
21.4
|
1.0
|
OG1
|
A:THR13
|
3.8
|
16.0
|
1.0
|
O
|
A:ASP386
|
4.1
|
13.8
|
1.0
|
O
|
A:HOH3043
|
4.2
|
23.7
|
1.0
|
O
|
A:HOH3354
|
4.2
|
18.8
|
1.0
|
O
|
A:HOH3250
|
4.2
|
29.1
|
1.0
|
CB
|
A:ASP386
|
4.2
|
14.6
|
1.0
|
CB
|
A:ASP390
|
4.3
|
13.9
|
1.0
|
O
|
A:THR10
|
4.3
|
18.1
|
1.0
|
C
|
A:ASP386
|
4.5
|
13.6
|
1.0
|
O
|
A:HOH3200
|
4.5
|
43.2
|
1.0
|
O
|
A:HOH3338
|
4.6
|
11.0
|
1.0
|
CB
|
A:THR10
|
4.8
|
18.9
|
1.0
|
O
|
A:HOH3228
|
4.9
|
38.5
|
1.0
|
O
|
A:HOH3060
|
4.9
|
21.1
|
1.0
|
CA
|
A:ASP386
|
4.9
|
14.3
|
1.0
|
CA
|
A:THR10
|
4.9
|
18.0
|
1.0
|
CB
|
A:THR13
|
5.0
|
16.2
|
1.0
|
N
|
A:ASN387
|
5.0
|
14.0
|
1.0
|
|
Zinc binding site 4 out
of 6 in 2ek9
Go back to
Zinc Binding Sites List in 2ek9
Zinc binding site 4 out
of 6 in the Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1004
b:19.7
occ:1.00
|
OD1
|
A:ASP386
|
2.0
|
13.9
|
1.0
|
O
|
A:THR13
|
2.1
|
18.6
|
1.0
|
O
|
A:HOH3338
|
2.1
|
11.0
|
1.0
|
O
|
A:HOH3354
|
2.2
|
18.8
|
1.0
|
OG1
|
A:THR13
|
2.2
|
16.0
|
1.0
|
CG
|
A:ASP386
|
3.1
|
15.4
|
1.0
|
CB
|
A:THR13
|
3.1
|
16.2
|
1.0
|
C
|
A:THR13
|
3.1
|
17.1
|
1.0
|
ZN
|
A:ZN1003
|
3.3
|
21.2
|
1.0
|
CA
|
A:THR13
|
3.4
|
17.2
|
1.0
|
OD2
|
A:ASP386
|
3.4
|
16.2
|
1.0
|
O
|
A:THR10
|
3.6
|
18.1
|
1.0
|
N
|
A:THR13
|
3.8
|
17.1
|
1.0
|
O
|
A:HOH3163
|
3.9
|
20.7
|
1.0
|
OD1
|
A:ASP390
|
4.0
|
14.5
|
1.0
|
O
|
A:HOH3030
|
4.1
|
27.0
|
1.0
|
O
|
A:HOH3121
|
4.2
|
39.9
|
1.0
|
N
|
A:ASP14
|
4.3
|
17.0
|
1.0
|
CB
|
A:ASP386
|
4.4
|
14.6
|
1.0
|
O
|
A:HOH3228
|
4.4
|
38.5
|
1.0
|
CG2
|
A:THR13
|
4.4
|
15.7
|
1.0
|
C
|
A:THR10
|
4.6
|
18.5
|
1.0
|
OD2
|
A:ASP390
|
4.7
|
15.5
|
1.0
|
CG
|
A:ASP390
|
4.8
|
13.5
|
1.0
|
C
|
A:ARG12
|
4.8
|
18.4
|
1.0
|
CA
|
A:ASP14
|
4.9
|
17.2
|
1.0
|
O
|
A:HOH3200
|
4.9
|
43.2
|
1.0
|
O
|
A:HOH3226
|
4.9
|
47.2
|
1.0
|
|
Zinc binding site 5 out
of 6 in 2ek9
Go back to
Zinc Binding Sites List in 2ek9
Zinc binding site 5 out
of 6 in the Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1005
b:24.4
occ:1.00
|
OE1
|
A:GLU383
|
2.0
|
17.9
|
1.0
|
O
|
A:HOH3240
|
2.1
|
23.8
|
1.0
|
CD
|
A:GLU383
|
2.7
|
16.4
|
1.0
|
OE2
|
A:GLU383
|
2.9
|
21.1
|
1.0
|
O
|
A:HOH3498
|
3.2
|
40.1
|
1.0
|
O
|
A:HOH3144
|
3.8
|
37.9
|
1.0
|
CG
|
A:GLU383
|
4.2
|
16.3
|
1.0
|
CB
|
A:GLU383
|
4.7
|
15.8
|
1.0
|
|
Zinc binding site 6 out
of 6 in 2ek9
Go back to
Zinc Binding Sites List in 2ek9
Zinc binding site 6 out
of 6 in the Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Aminopeptidase From Aneurinibacillus Sp. Strain Am-1 with Bestatin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1006
b:21.2
occ:1.00
|
NE2
|
A:HIS204
|
2.0
|
15.7
|
1.0
|
O
|
A:HOH3029
|
2.7
|
21.0
|
1.0
|
CD2
|
A:HIS204
|
2.9
|
10.7
|
1.0
|
CE1
|
A:HIS204
|
3.1
|
12.8
|
1.0
|
O
|
A:HOH3210
|
3.3
|
31.3
|
1.0
|
CG
|
A:HIS204
|
4.1
|
12.7
|
1.0
|
ND1
|
A:HIS204
|
4.2
|
14.4
|
1.0
|
CG2
|
A:THR202
|
4.4
|
16.0
|
1.0
|
CB
|
A:PRO59
|
4.5
|
14.0
|
1.0
|
CD1
|
A:LEU38
|
5.0
|
20.0
|
1.0
|
|
Reference:
M.Akioka,
H.Nakano,
Y.Tsujimoto,
H.Matsui,
T.Nakatsu,
H.Kato,
K.Watanabe.
Structural Characterization of A Novel Bacterial Aminopeptidase with An Apical Domain From Aneurinibacillus Sp. Strain Am-1 To Be Published.
Page generated: Wed Oct 16 23:13:34 2024
|