Zinc in PDB 6hc7: The Crystal Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution)
Protein crystallography data
The structure of The Crystal Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution), PDB code: 6hc7
was solved by
R.Alhadeff,
S.Lansky,
H.Feinberg,
Y.Shoham,
G.Shoham,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
73.92 /
2.50
|
Space group
|
P 63
|
Cell size a, b, c (Å), α, β, γ (°)
|
225.833,
225.833,
42.654,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
17.8 /
25.1
|
Other elements in 6hc7:
The structure of The Crystal Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution) also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the The Crystal Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution)
(pdb code 6hc7). 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 Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution), PDB code: 6hc7:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 6hc7
Go back to
Zinc Binding Sites List in 6hc7
Zinc binding site 1 out
of 6 in the The Crystal Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution)
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 Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn501
b:41.2
occ:1.00
|
O
|
A:HOH607
|
2.0
|
31.2
|
1.0
|
OD1
|
A:ASP262
|
2.1
|
30.3
|
1.0
|
OD2
|
A:ASP323
|
2.2
|
27.8
|
1.0
|
OD1
|
A:ASP323
|
2.3
|
27.3
|
1.0
|
NE2
|
A:HIS250
|
2.3
|
28.6
|
1.0
|
CG
|
A:ASP323
|
2.5
|
30.0
|
1.0
|
CG
|
A:ASP262
|
3.0
|
25.1
|
1.0
|
CD2
|
A:HIS250
|
3.2
|
25.9
|
1.0
|
CE1
|
A:HIS250
|
3.4
|
29.1
|
1.0
|
OD2
|
A:ASP262
|
3.5
|
21.7
|
1.0
|
ZN
|
A:ZN502
|
3.5
|
43.8
|
1.0
|
CB
|
A:ASN263
|
4.0
|
27.9
|
1.0
|
CB
|
A:ASP323
|
4.1
|
29.9
|
1.0
|
OE2
|
A:GLU294
|
4.1
|
34.3
|
1.0
|
OE2
|
A:GLU452
|
4.1
|
37.7
|
1.0
|
CB
|
A:ASP262
|
4.3
|
26.7
|
1.0
|
CG
|
A:HIS250
|
4.4
|
32.8
|
1.0
|
ND1
|
A:HIS250
|
4.4
|
27.9
|
1.0
|
CD
|
A:GLU294
|
4.5
|
31.1
|
1.0
|
CG
|
A:MET324
|
4.5
|
28.8
|
1.0
|
OE1
|
A:GLU295
|
4.5
|
25.2
|
1.0
|
SD
|
A:MET324
|
4.5
|
40.7
|
1.0
|
CG
|
A:ASN263
|
4.6
|
30.3
|
1.0
|
CA
|
A:ASP262
|
4.6
|
30.4
|
1.0
|
OE1
|
A:GLU294
|
4.6
|
32.1
|
1.0
|
ND2
|
A:ASN263
|
4.7
|
25.9
|
1.0
|
OE2
|
A:GLU295
|
4.9
|
31.2
|
1.0
|
CA
|
A:ASP323
|
4.9
|
30.6
|
1.0
|
OE1
|
A:GLU452
|
4.9
|
33.8
|
1.0
|
CD
|
A:GLU452
|
4.9
|
36.9
|
1.0
|
C
|
A:ASP262
|
5.0
|
29.2
|
1.0
|
OG
|
A:SER371
|
5.0
|
34.3
|
1.0
|
|
Zinc binding site 2 out
of 6 in 6hc7
Go back to
Zinc Binding Sites List in 6hc7
Zinc binding site 2 out
of 6 in the The Crystal Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution)
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 Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn502
b:43.8
occ:1.00
|
OD2
|
A:ASP262
|
2.0
|
21.7
|
1.0
|
NE2
|
A:HIS401
|
2.3
|
27.4
|
1.0
|
OE2
|
A:GLU295
|
2.3
|
31.2
|
1.0
|
OE1
|
A:GLU452
|
2.5
|
33.8
|
1.0
|
OE1
|
A:GLU295
|
2.6
|
25.2
|
1.0
|
O
|
A:HOH607
|
2.6
|
31.2
|
1.0
|
CD
|
A:GLU295
|
2.8
|
29.4
|
1.0
|
CG
|
A:ASP262
|
3.0
|
25.1
|
1.0
|
OD1
|
A:ASP262
|
3.3
|
30.3
|
1.0
|
CD2
|
A:HIS401
|
3.3
|
28.5
|
1.0
|
CE1
|
A:HIS401
|
3.3
|
29.1
|
1.0
|
CD
|
A:GLU452
|
3.3
|
36.9
|
1.0
|
OE2
|
A:GLU452
|
3.4
|
37.7
|
1.0
|
ZN
|
A:ZN501
|
3.5
|
41.2
|
1.0
|
CE1
|
A:TYR400
|
3.9
|
34.7
|
1.0
|
O
|
A:HOH617
|
4.2
|
29.9
|
1.0
|
CG
|
A:GLU295
|
4.2
|
36.2
|
1.0
|
CB
|
A:ASP262
|
4.3
|
26.7
|
1.0
|
ND1
|
A:HIS401
|
4.4
|
33.4
|
1.0
|
OE2
|
A:GLU294
|
4.4
|
34.3
|
1.0
|
OH
|
A:TYR400
|
4.4
|
46.4
|
1.0
|
CG
|
A:HIS401
|
4.5
|
34.8
|
1.0
|
CG1
|
A:VAL254
|
4.6
|
27.5
|
1.0
|
CZ
|
A:TYR400
|
4.6
|
38.5
|
1.0
|
NE2
|
A:HIS250
|
4.6
|
28.6
|
1.0
|
CE1
|
A:HIS250
|
4.7
|
29.1
|
1.0
|
CD1
|
A:TYR400
|
4.7
|
37.7
|
1.0
|
CG
|
A:GLU452
|
4.8
|
39.4
|
1.0
|
|
Zinc binding site 3 out
of 6 in 6hc7
Go back to
Zinc Binding Sites List in 6hc7
Zinc binding site 3 out
of 6 in the The Crystal Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution)
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 Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn501
b:32.8
occ:1.00
|
O
|
B:HOH606
|
2.1
|
22.4
|
1.0
|
NE2
|
B:HIS250
|
2.1
|
23.8
|
1.0
|
OD1
|
B:ASP262
|
2.2
|
21.2
|
1.0
|
OD2
|
B:ASP323
|
2.3
|
24.4
|
1.0
|
OD1
|
B:ASP323
|
2.3
|
26.5
|
1.0
|
O
|
B:HOH740
|
2.6
|
31.0
|
1.0
|
CG
|
B:ASP323
|
2.6
|
26.4
|
1.0
|
CE1
|
B:HIS250
|
3.1
|
19.2
|
1.0
|
CD2
|
B:HIS250
|
3.2
|
19.8
|
1.0
|
CG
|
B:ASP262
|
3.2
|
19.4
|
1.0
|
ZN
|
B:ZN502
|
3.6
|
34.6
|
1.0
|
OD2
|
B:ASP262
|
3.6
|
22.3
|
1.0
|
OE2
|
B:GLU294
|
3.8
|
28.2
|
1.0
|
CB
|
B:ASN263
|
4.1
|
20.1
|
1.0
|
CB
|
B:ASP323
|
4.1
|
24.3
|
1.0
|
ND1
|
B:HIS250
|
4.2
|
19.2
|
1.0
|
OE2
|
B:GLU452
|
4.3
|
36.2
|
1.0
|
CG
|
B:HIS250
|
4.3
|
19.5
|
1.0
|
CD
|
B:GLU294
|
4.3
|
22.8
|
1.0
|
O
|
B:HOH654
|
4.3
|
36.9
|
1.0
|
CG
|
B:MET324
|
4.4
|
24.7
|
1.0
|
OE1
|
B:GLU295
|
4.4
|
22.8
|
1.0
|
CB
|
B:ASP262
|
4.5
|
18.9
|
1.0
|
OE1
|
B:GLU452
|
4.5
|
35.5
|
1.0
|
OE1
|
B:GLU294
|
4.5
|
19.1
|
1.0
|
CG
|
B:ASN263
|
4.5
|
20.7
|
1.0
|
SD
|
B:MET324
|
4.6
|
25.1
|
1.0
|
CA
|
B:ASP262
|
4.7
|
21.5
|
1.0
|
OG
|
B:SER371
|
4.8
|
21.2
|
1.0
|
CD
|
B:GLU452
|
4.8
|
34.9
|
1.0
|
ND2
|
B:ASN263
|
4.8
|
22.0
|
1.0
|
CA
|
B:ASP323
|
4.9
|
22.2
|
1.0
|
C
|
B:ASP262
|
5.0
|
21.5
|
1.0
|
|
Zinc binding site 4 out
of 6 in 6hc7
Go back to
Zinc Binding Sites List in 6hc7
Zinc binding site 4 out
of 6 in the The Crystal Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution)
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 Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn502
b:34.6
occ:1.00
|
OE1
|
B:GLU452
|
2.2
|
35.5
|
1.0
|
NE2
|
B:HIS401
|
2.2
|
20.0
|
1.0
|
OD2
|
B:ASP262
|
2.3
|
22.3
|
1.0
|
OE1
|
B:GLU295
|
2.5
|
22.8
|
1.0
|
O
|
B:HOH606
|
2.6
|
22.4
|
1.0
|
OE2
|
B:GLU295
|
2.6
|
26.1
|
1.0
|
CD
|
B:GLU295
|
2.8
|
28.2
|
1.0
|
CD
|
B:GLU452
|
3.1
|
34.9
|
1.0
|
CG
|
B:ASP262
|
3.2
|
19.4
|
1.0
|
CE1
|
B:HIS401
|
3.2
|
22.3
|
1.0
|
CD2
|
B:HIS401
|
3.3
|
22.2
|
1.0
|
OD1
|
B:ASP262
|
3.4
|
21.2
|
1.0
|
OE2
|
B:GLU452
|
3.5
|
36.2
|
1.0
|
ZN
|
B:ZN501
|
3.6
|
32.8
|
1.0
|
O
|
B:HOH740
|
3.6
|
31.0
|
1.0
|
CE1
|
B:TYR400
|
3.8
|
23.7
|
1.0
|
OH
|
B:TYR400
|
4.0
|
26.6
|
1.0
|
O
|
B:HOH646
|
4.0
|
20.9
|
1.0
|
CG
|
B:GLU452
|
4.2
|
39.5
|
1.0
|
CZ
|
B:TYR400
|
4.3
|
27.6
|
1.0
|
ND1
|
B:HIS401
|
4.3
|
24.0
|
1.0
|
OE2
|
B:GLU294
|
4.3
|
28.2
|
1.0
|
CG
|
B:GLU295
|
4.3
|
26.0
|
1.0
|
CG
|
B:HIS401
|
4.4
|
25.9
|
1.0
|
CB
|
B:ASP262
|
4.5
|
18.9
|
1.0
|
O
|
B:HOH618
|
4.6
|
28.8
|
1.0
|
CG1
|
B:VAL254
|
4.6
|
22.2
|
1.0
|
CE1
|
B:HIS250
|
4.6
|
19.2
|
1.0
|
NE2
|
B:HIS250
|
4.7
|
23.8
|
1.0
|
CD1
|
B:TYR400
|
4.8
|
26.4
|
1.0
|
|
Zinc binding site 5 out
of 6 in 6hc7
Go back to
Zinc Binding Sites List in 6hc7
Zinc binding site 5 out
of 6 in the The Crystal Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution)
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 Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn501
b:37.3
occ:1.00
|
OD1
|
C:ASP262
|
2.0
|
22.2
|
1.0
|
O
|
C:HOH609
|
2.2
|
29.7
|
1.0
|
OD1
|
C:ASP323
|
2.3
|
23.3
|
1.0
|
NE2
|
C:HIS250
|
2.3
|
25.7
|
1.0
|
OD2
|
C:ASP323
|
2.4
|
27.0
|
1.0
|
CG
|
C:ASP323
|
2.6
|
23.7
|
1.0
|
CG
|
C:ASP262
|
3.0
|
24.2
|
1.0
|
CE1
|
C:HIS250
|
3.1
|
27.5
|
1.0
|
CD2
|
C:HIS250
|
3.4
|
25.7
|
1.0
|
OD2
|
C:ASP262
|
3.5
|
32.9
|
1.0
|
ZN
|
C:ZN502
|
3.7
|
45.5
|
1.0
|
OE2
|
C:GLU294
|
4.0
|
35.8
|
1.0
|
CB
|
C:ASN263
|
4.0
|
21.1
|
1.0
|
CB
|
C:ASP323
|
4.1
|
23.2
|
1.0
|
OE2
|
C:GLU452
|
4.2
|
38.0
|
1.0
|
OE2
|
C:GLU295
|
4.2
|
32.4
|
1.0
|
CB
|
C:ASP262
|
4.3
|
29.1
|
1.0
|
ND1
|
C:HIS250
|
4.3
|
26.6
|
1.0
|
CD
|
C:GLU294
|
4.4
|
34.6
|
1.0
|
CG
|
C:MET324
|
4.4
|
26.4
|
1.0
|
CG
|
C:HIS250
|
4.5
|
26.2
|
1.0
|
OE1
|
C:GLU294
|
4.5
|
33.2
|
1.0
|
CG
|
C:ASN263
|
4.6
|
27.4
|
1.0
|
OE1
|
C:GLU452
|
4.6
|
36.6
|
1.0
|
CA
|
C:ASP262
|
4.7
|
29.1
|
1.0
|
OG
|
C:SER371
|
4.7
|
32.0
|
1.0
|
SD
|
C:MET324
|
4.8
|
32.5
|
1.0
|
CD
|
C:GLU452
|
4.9
|
39.1
|
1.0
|
CA
|
C:ASP323
|
4.9
|
24.5
|
1.0
|
C
|
C:ASP262
|
4.9
|
28.4
|
1.0
|
CD
|
C:GLU295
|
5.0
|
34.2
|
1.0
|
ND2
|
C:ASN263
|
5.0
|
25.8
|
1.0
|
|
Zinc binding site 6 out
of 6 in 6hc7
Go back to
Zinc Binding Sites List in 6hc7
Zinc binding site 6 out
of 6 in the The Crystal Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution)
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 Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn502
b:45.5
occ:1.00
|
NE2
|
C:HIS401
|
2.1
|
29.5
|
1.0
|
OD2
|
C:ASP262
|
2.2
|
32.9
|
1.0
|
O
|
C:HOH609
|
2.2
|
29.7
|
1.0
|
OE1
|
C:GLU452
|
2.3
|
36.6
|
1.0
|
OE2
|
C:GLU295
|
2.4
|
32.4
|
1.0
|
OE1
|
C:GLU295
|
2.7
|
36.9
|
1.0
|
CD
|
C:GLU295
|
2.9
|
34.2
|
1.0
|
CE1
|
C:HIS401
|
3.0
|
27.1
|
1.0
|
CD2
|
C:HIS401
|
3.2
|
29.1
|
1.0
|
CG
|
C:ASP262
|
3.2
|
24.2
|
1.0
|
CD
|
C:GLU452
|
3.2
|
39.1
|
1.0
|
OE2
|
C:GLU452
|
3.5
|
38.0
|
1.0
|
OD1
|
C:ASP262
|
3.6
|
22.2
|
1.0
|
ZN
|
C:ZN501
|
3.7
|
37.3
|
1.0
|
CE1
|
C:TYR400
|
3.7
|
32.9
|
1.0
|
OH
|
C:TYR400
|
3.9
|
40.6
|
1.0
|
CZ
|
C:TYR400
|
4.1
|
35.3
|
1.0
|
ND1
|
C:HIS401
|
4.2
|
32.8
|
1.0
|
CG
|
C:HIS401
|
4.3
|
34.5
|
1.0
|
O
|
C:HOH619
|
4.3
|
26.3
|
1.0
|
OE2
|
C:GLU294
|
4.4
|
35.8
|
1.0
|
CG
|
C:GLU295
|
4.5
|
31.6
|
1.0
|
CB
|
C:ASP262
|
4.5
|
29.1
|
1.0
|
CG
|
C:GLU452
|
4.6
|
43.5
|
1.0
|
CD1
|
C:TYR400
|
4.6
|
32.8
|
1.0
|
CG1
|
C:VAL254
|
4.7
|
29.0
|
1.0
|
CE1
|
C:HIS250
|
4.9
|
27.5
|
1.0
|
CB
|
C:GLU452
|
4.9
|
43.5
|
1.0
|
|
Reference:
R.Alhadeff,
R.Faygenboim,
S.Lansky,
E.Rogoulenko,
T.Cohen,
Y.Fundoiano-Hershcovitz,
H.Feinberg,
Y.Shoham,
G.Shoham.
The Crystal Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (Medium Resolution) To Be Published.
Page generated: Mon Oct 28 22:46:55 2024
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