Zinc in PDB 4gk8: Crystal Structure of Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate
Enzymatic activity of Crystal Structure of Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate
All present enzymatic activity of Crystal Structure of Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate:
3.1.3.15;
Protein crystallography data
The structure of Crystal Structure of Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate, PDB code: 4gk8
was solved by
A.A.Fedorov,
E.V.Fedorov,
S.Ghodge,
F.M.Raushel,
S.C.Almo,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
43.31 /
1.93
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
85.860,
86.622,
45.093,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.2 /
19.6
|
Other elements in 4gk8:
The structure of Crystal Structure of Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate
(pdb code 4gk8). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Crystal Structure of Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate, PDB code: 4gk8:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 4gk8
Go back to
Zinc Binding Sites List in 4gk8
Zinc binding site 1 out
of 4 in the Crystal Structure of Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate
 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 Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:15.9
occ:0.88
|
O2
|
A:GK8305
|
1.9
|
21.9
|
0.8
|
OE2
|
A:GLU81
|
2.0
|
17.1
|
1.0
|
O
|
A:HOH575
|
2.1
|
23.9
|
1.0
|
NE2
|
A:HIS109
|
2.1
|
19.3
|
1.0
|
NE2
|
A:HIS154
|
2.1
|
17.5
|
1.0
|
CE1
|
A:HIS109
|
3.0
|
18.4
|
1.0
|
CD
|
A:GLU81
|
3.0
|
19.0
|
1.0
|
CD2
|
A:HIS154
|
3.1
|
15.0
|
1.0
|
CD2
|
A:HIS109
|
3.1
|
17.7
|
1.0
|
CE1
|
A:HIS154
|
3.2
|
19.0
|
1.0
|
AS
|
A:GK8305
|
3.2
|
24.1
|
0.8
|
OE1
|
A:GLU81
|
3.3
|
16.3
|
1.0
|
ZN
|
A:ZN303
|
3.7
|
17.4
|
0.8
|
O3
|
A:GK8305
|
3.7
|
21.4
|
0.8
|
OG
|
A:SER107
|
3.9
|
19.9
|
1.0
|
CE1
|
A:TYR157
|
4.0
|
20.6
|
1.0
|
ND1
|
A:HIS109
|
4.1
|
17.2
|
1.0
|
O1
|
A:GK8305
|
4.2
|
21.2
|
0.8
|
CB
|
A:SER107
|
4.2
|
15.2
|
1.0
|
CG
|
A:HIS109
|
4.2
|
17.4
|
1.0
|
CG
|
A:HIS154
|
4.2
|
15.4
|
1.0
|
ND1
|
A:HIS154
|
4.2
|
16.1
|
1.0
|
CG
|
A:GLU81
|
4.3
|
18.2
|
1.0
|
CE1
|
A:HIS42
|
4.3
|
16.7
|
1.0
|
CD1
|
A:TYR157
|
4.3
|
18.9
|
1.0
|
N
|
A:GK8305
|
4.4
|
21.1
|
0.8
|
CE1
|
A:HIS9
|
4.5
|
16.0
|
1.0
|
OD2
|
A:ASP228
|
4.5
|
17.9
|
1.0
|
NE2
|
A:HIS9
|
4.6
|
16.5
|
1.0
|
O4
|
A:GK8305
|
4.6
|
19.2
|
0.8
|
CZ
|
A:TYR157
|
4.8
|
22.3
|
1.0
|
|
Zinc binding site 2 out
of 4 in 4gk8
Go back to
Zinc Binding Sites List in 4gk8
Zinc binding site 2 out
of 4 in the Crystal Structure of Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate
 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 Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn302
b:19.9
occ:1.00
|
NE2
|
A:HIS42
|
2.1
|
16.8
|
1.0
|
OD2
|
A:ASP17
|
2.1
|
16.9
|
1.0
|
NE2
|
A:HIS230
|
2.1
|
18.5
|
1.0
|
O4
|
A:GK8305
|
2.2
|
19.2
|
0.8
|
O3
|
A:GK8305
|
2.7
|
21.4
|
0.8
|
CG
|
A:ASP17
|
2.8
|
16.6
|
1.0
|
OD1
|
A:ASP17
|
2.9
|
16.2
|
1.0
|
AS
|
A:GK8305
|
3.1
|
24.1
|
0.8
|
CE1
|
A:HIS42
|
3.1
|
16.7
|
1.0
|
CD2
|
A:HIS42
|
3.1
|
14.5
|
1.0
|
CE1
|
A:HIS230
|
3.1
|
21.7
|
1.0
|
CD2
|
A:HIS230
|
3.1
|
16.8
|
1.0
|
C
|
A:GK8305
|
3.3
|
28.7
|
0.8
|
CA
|
A:GK8305
|
3.8
|
24.8
|
0.8
|
NE2
|
A:HIS11
|
4.1
|
15.7
|
1.0
|
ND1
|
A:HIS42
|
4.2
|
16.4
|
1.0
|
ND1
|
A:HIS230
|
4.2
|
15.2
|
1.0
|
CG
|
A:HIS42
|
4.2
|
16.0
|
1.0
|
CG
|
A:HIS230
|
4.2
|
17.6
|
1.0
|
O1
|
A:GK8305
|
4.2
|
21.2
|
0.8
|
CE1
|
A:HIS11
|
4.2
|
18.3
|
1.0
|
O2
|
A:GK8305
|
4.2
|
21.9
|
0.8
|
CD2
|
A:HIS11
|
4.3
|
15.0
|
1.0
|
O
|
A:HOH557
|
4.3
|
39.2
|
1.0
|
CB
|
A:ASP17
|
4.3
|
17.6
|
1.0
|
ZN
|
A:ZN303
|
4.4
|
17.4
|
0.8
|
ND1
|
A:HIS11
|
4.4
|
16.1
|
1.0
|
N
|
A:GK8305
|
4.5
|
21.1
|
0.8
|
CG
|
A:HIS11
|
4.5
|
15.9
|
1.0
|
CD2
|
A:GK8305
|
4.8
|
27.6
|
0.8
|
CE1
|
A:PHE52
|
4.9
|
18.7
|
1.0
|
|
Zinc binding site 3 out
of 4 in 4gk8
Go back to
Zinc Binding Sites List in 4gk8
Zinc binding site 3 out
of 4 in the Crystal Structure of Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate
 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 Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn303
b:17.4
occ:0.84
|
O3
|
A:GK8305
|
1.8
|
21.4
|
0.8
|
O
|
A:HOH575
|
2.1
|
23.9
|
1.0
|
NE2
|
A:HIS9
|
2.1
|
16.5
|
1.0
|
NE2
|
A:HIS11
|
2.2
|
15.7
|
1.0
|
OE1
|
A:GLU81
|
2.2
|
16.3
|
1.0
|
OD1
|
A:ASP228
|
2.3
|
19.9
|
1.0
|
CE1
|
A:HIS11
|
3.0
|
18.3
|
1.0
|
CE1
|
A:HIS9
|
3.1
|
16.0
|
1.0
|
CD2
|
A:HIS9
|
3.1
|
16.9
|
1.0
|
CD
|
A:GLU81
|
3.1
|
19.0
|
1.0
|
CG
|
A:ASP228
|
3.2
|
20.7
|
1.0
|
CD2
|
A:HIS11
|
3.2
|
15.0
|
1.0
|
AS
|
A:GK8305
|
3.2
|
24.1
|
0.8
|
OD2
|
A:ASP228
|
3.4
|
17.9
|
1.0
|
OE2
|
A:GLU81
|
3.5
|
17.1
|
1.0
|
ZN
|
A:ZN301
|
3.7
|
15.9
|
0.9
|
O2
|
A:GK8305
|
3.9
|
21.9
|
0.8
|
CE1
|
A:HIS42
|
3.9
|
16.7
|
1.0
|
O1
|
A:GK8305
|
4.1
|
21.2
|
0.8
|
ND1
|
A:HIS9
|
4.2
|
17.1
|
1.0
|
ND1
|
A:HIS11
|
4.2
|
16.1
|
1.0
|
CE1
|
A:HIS230
|
4.2
|
21.7
|
1.0
|
CG
|
A:HIS9
|
4.2
|
14.4
|
1.0
|
NE2
|
A:HIS42
|
4.2
|
16.8
|
1.0
|
CG
|
A:HIS11
|
4.3
|
15.9
|
1.0
|
ZN
|
A:ZN302
|
4.4
|
19.9
|
1.0
|
CG
|
A:GLU81
|
4.4
|
18.2
|
1.0
|
CB
|
A:ASP228
|
4.5
|
18.7
|
1.0
|
NE2
|
A:HIS230
|
4.6
|
18.5
|
1.0
|
O4
|
A:GK8305
|
4.6
|
19.2
|
0.8
|
CB
|
A:GLU81
|
4.7
|
17.5
|
1.0
|
ND1
|
A:HIS42
|
4.8
|
16.4
|
1.0
|
CA
|
A:ASP228
|
4.8
|
16.1
|
1.0
|
|
Zinc binding site 4 out
of 4 in 4gk8
Go back to
Zinc Binding Sites List in 4gk8
Zinc binding site 4 out
of 4 in the Crystal Structure of Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate
 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 Histidinol Phosphate Phosphatase (Hisk) From Lactococcus Lactis Subsp. Lactis IL1403 Complexed with Zn and L- Histidinol Arsenate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn304
b:21.4
occ:1.00
|
N3
|
A:IMD309
|
2.0
|
21.6
|
1.0
|
NE2
|
A:HIS32
|
2.0
|
20.7
|
1.0
|
NE2
|
A:HIS240
|
2.0
|
22.4
|
1.0
|
CL
|
A:CL306
|
2.2
|
24.2
|
1.0
|
C2
|
A:IMD309
|
2.9
|
23.7
|
1.0
|
CD2
|
A:HIS240
|
2.9
|
21.0
|
1.0
|
CD2
|
A:HIS32
|
3.0
|
16.2
|
1.0
|
CE1
|
A:HIS32
|
3.0
|
18.6
|
1.0
|
CE1
|
A:HIS240
|
3.1
|
19.2
|
1.0
|
C4
|
A:IMD309
|
3.1
|
21.8
|
1.0
|
N1
|
A:IMD309
|
4.1
|
28.4
|
1.0
|
CG
|
A:HIS32
|
4.1
|
18.0
|
1.0
|
ND1
|
A:HIS32
|
4.1
|
17.4
|
1.0
|
CG
|
A:HIS240
|
4.1
|
20.0
|
1.0
|
ND1
|
A:HIS240
|
4.2
|
19.4
|
1.0
|
C5
|
A:IMD309
|
4.2
|
23.2
|
1.0
|
CE3
|
A:TRP236
|
4.3
|
20.7
|
1.0
|
CZ3
|
A:TRP236
|
4.8
|
19.8
|
1.0
|
CD2
|
A:TRP236
|
4.9
|
17.9
|
1.0
|
|
Reference:
S.V.Ghodge,
A.A.Fedorov,
E.V.Fedorov,
B.Hillerich,
R.Seidel,
S.C.Almo,
F.M.Raushel.
Structural and Mechanistic Characterization of L-Histidinol Phosphate Phosphatase From the Polymerase and Histidinol Phosphatase Family of Proteins. Biochemistry V. 52 1101 2013.
ISSN: ISSN 0006-2960
PubMed: 23327428
DOI: 10.1021/BI301496P
Page generated: Sat Oct 26 23:19:31 2024
|