Iron in PDB 6hwr: Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate
Enzymatic activity of Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate
All present enzymatic activity of Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate:
3.1.3.2;
Protein crystallography data
The structure of Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate, PDB code: 6hwr
was solved by
D.Feder,
L.R.Gahan,
R.P.Mcgeary,
L.W.Guddat,
G.Schenk,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.97 /
1.95
|
Space group
|
P 31 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
126.242,
126.242,
296.877,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
16.3 /
19.9
|
Other elements in 6hwr:
The structure of Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate
(pdb code 6hwr). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate, PDB code: 6hwr:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 6hwr
Go back to
Iron Binding Sites List in 6hwr
Iron binding site 1 out
of 4 in the Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe502
b:21.7
occ:0.81
|
OH
|
C:TYR167
|
1.9
|
16.4
|
1.0
|
OD2
|
C:ASP135
|
2.1
|
18.6
|
1.0
|
O02
|
C:H1T520
|
2.2
|
15.7
|
0.6
|
O03
|
C:H1T520
|
2.3
|
22.3
|
0.6
|
NE2
|
C:HIS325
|
2.3
|
17.8
|
1.0
|
OD2
|
C:ASP164
|
2.3
|
14.2
|
1.0
|
V01
|
C:H1T520
|
2.9
|
28.8
|
0.6
|
CG
|
C:ASP135
|
3.0
|
12.9
|
1.0
|
CZ
|
C:TYR167
|
3.1
|
15.6
|
1.0
|
CE1
|
C:HIS325
|
3.3
|
19.5
|
1.0
|
CG
|
C:ASP164
|
3.3
|
13.8
|
1.0
|
CD2
|
C:HIS325
|
3.3
|
13.5
|
1.0
|
CB
|
C:ASP135
|
3.4
|
12.4
|
1.0
|
ZN
|
C:ZN501
|
3.5
|
20.8
|
0.9
|
CB
|
C:ASP164
|
3.6
|
12.5
|
1.0
|
CE2
|
C:TYR167
|
3.6
|
14.0
|
1.0
|
O01
|
C:H1T520
|
3.8
|
22.4
|
0.6
|
O
|
C:HIS323
|
4.0
|
17.7
|
1.0
|
O04
|
C:H1T520
|
4.1
|
21.2
|
0.6
|
OD1
|
C:ASP135
|
4.2
|
13.5
|
1.0
|
CE1
|
C:TYR167
|
4.2
|
14.8
|
1.0
|
CD2
|
C:HIS202
|
4.3
|
16.7
|
1.0
|
CA
|
C:ASP135
|
4.3
|
10.7
|
1.0
|
O07
|
C:H1T520
|
4.4
|
31.9
|
0.6
|
CA
|
C:HIS323
|
4.4
|
14.1
|
1.0
|
ND1
|
C:HIS325
|
4.4
|
17.8
|
1.0
|
OD1
|
C:ASP164
|
4.4
|
12.9
|
1.0
|
CG
|
C:HIS325
|
4.5
|
15.3
|
1.0
|
CE1
|
C:HIS286
|
4.5
|
12.1
|
1.0
|
NE2
|
C:HIS202
|
4.6
|
16.9
|
1.0
|
NE2
|
C:HIS286
|
4.6
|
15.7
|
1.0
|
C
|
C:HIS323
|
4.6
|
15.9
|
1.0
|
O05
|
C:H1T520
|
4.8
|
31.2
|
0.6
|
N
|
C:HIS323
|
4.8
|
12.5
|
1.0
|
CB
|
C:ASN364
|
4.8
|
14.8
|
1.0
|
CD2
|
C:TYR167
|
5.0
|
11.2
|
1.0
|
|
Iron binding site 2 out
of 4 in 6hwr
Go back to
Iron Binding Sites List in 6hwr
Iron binding site 2 out
of 4 in the Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe502
b:21.9
occ:0.80
|
O03
|
B:VV6521
|
1.9
|
22.9
|
0.6
|
OH
|
B:TYR167
|
2.0
|
18.4
|
1.0
|
OD2
|
B:ASP135
|
2.0
|
14.3
|
1.0
|
O02
|
B:VV6521
|
2.3
|
19.2
|
0.6
|
OD1
|
B:ASP164
|
2.3
|
15.5
|
1.0
|
NE2
|
B:HIS325
|
2.4
|
19.2
|
1.0
|
V01
|
B:VV6521
|
2.8
|
29.8
|
0.6
|
CG
|
B:ASP135
|
3.0
|
17.1
|
1.0
|
CZ
|
B:TYR167
|
3.1
|
15.2
|
1.0
|
CG
|
B:ASP164
|
3.3
|
17.2
|
1.0
|
CD2
|
B:HIS325
|
3.3
|
17.6
|
1.0
|
CB
|
B:ASP135
|
3.4
|
13.5
|
1.0
|
CE1
|
B:HIS325
|
3.5
|
19.9
|
1.0
|
ZN
|
B:ZN501
|
3.5
|
23.9
|
1.0
|
CB
|
B:ASP164
|
3.6
|
15.3
|
1.0
|
CE1
|
B:TYR167
|
3.6
|
15.9
|
1.0
|
O04
|
B:VV6521
|
3.8
|
23.1
|
0.6
|
O07
|
B:VV6521
|
4.1
|
32.5
|
0.6
|
O
|
B:HIS323
|
4.1
|
16.5
|
1.0
|
OD1
|
B:ASP135
|
4.1
|
19.0
|
1.0
|
O01
|
B:VV6521
|
4.1
|
26.6
|
0.6
|
CD2
|
B:HIS202
|
4.2
|
20.6
|
1.0
|
CE2
|
B:TYR167
|
4.2
|
15.1
|
1.0
|
CA
|
B:ASP135
|
4.3
|
12.2
|
1.0
|
OD2
|
B:ASP164
|
4.4
|
14.4
|
1.0
|
CA
|
B:HIS323
|
4.5
|
16.4
|
1.0
|
NE2
|
B:HIS202
|
4.5
|
23.0
|
1.0
|
CG
|
B:HIS325
|
4.5
|
19.8
|
1.0
|
ND1
|
B:HIS325
|
4.6
|
19.2
|
1.0
|
CE1
|
B:HIS286
|
4.6
|
13.2
|
1.0
|
NE2
|
B:HIS286
|
4.6
|
16.2
|
1.0
|
C
|
B:HIS323
|
4.7
|
17.3
|
1.0
|
CB
|
B:ASN364
|
4.8
|
16.0
|
1.0
|
N
|
B:HIS323
|
4.9
|
14.6
|
1.0
|
CD1
|
B:TYR167
|
5.0
|
17.9
|
1.0
|
|
Iron binding site 3 out
of 4 in 6hwr
Go back to
Iron Binding Sites List in 6hwr
Iron binding site 3 out
of 4 in the Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:19.8
occ:0.78
|
OH
|
A:TYR167
|
2.0
|
16.9
|
1.0
|
OD2
|
A:ASP135
|
2.0
|
16.9
|
1.0
|
O3
|
A:H1Q527
|
2.1
|
22.5
|
0.8
|
OD2
|
A:ASP164
|
2.3
|
16.1
|
1.0
|
O2
|
A:H1Q527
|
2.3
|
28.8
|
0.8
|
NE2
|
A:HIS325
|
2.5
|
21.4
|
1.0
|
V1
|
A:H1Q527
|
3.0
|
35.9
|
0.8
|
CG
|
A:ASP135
|
3.0
|
13.4
|
1.0
|
CZ
|
A:TYR167
|
3.1
|
18.3
|
1.0
|
CG
|
A:ASP164
|
3.3
|
14.7
|
1.0
|
CD2
|
A:HIS325
|
3.4
|
18.7
|
1.0
|
CB
|
A:ASP135
|
3.4
|
11.4
|
1.0
|
ZN
|
A:ZN501
|
3.5
|
20.8
|
0.9
|
CE1
|
A:HIS325
|
3.5
|
22.6
|
1.0
|
CB
|
A:ASP164
|
3.6
|
13.2
|
1.0
|
CE2
|
A:TYR167
|
3.6
|
18.3
|
1.0
|
O5
|
A:H1Q527
|
3.9
|
25.5
|
0.8
|
O
|
A:HIS323
|
4.0
|
14.9
|
1.0
|
O4
|
A:H1Q527
|
4.1
|
27.1
|
0.8
|
OD1
|
A:ASP135
|
4.2
|
16.4
|
1.0
|
CD2
|
A:HIS202
|
4.2
|
20.9
|
1.0
|
CE1
|
A:TYR167
|
4.2
|
14.5
|
1.0
|
CA
|
A:ASP135
|
4.4
|
14.2
|
1.0
|
CA
|
A:HIS323
|
4.4
|
12.6
|
1.0
|
OD1
|
A:ASP164
|
4.4
|
13.5
|
1.0
|
CG
|
A:HIS325
|
4.6
|
20.4
|
1.0
|
CE1
|
A:HIS286
|
4.6
|
12.6
|
1.0
|
NE2
|
A:HIS286
|
4.6
|
12.3
|
1.0
|
ND1
|
A:HIS325
|
4.6
|
20.8
|
1.0
|
NE2
|
A:HIS202
|
4.6
|
17.0
|
1.0
|
C
|
A:HIS323
|
4.6
|
16.0
|
1.0
|
O9
|
A:H1Q527
|
4.7
|
38.2
|
0.8
|
N
|
A:HIS323
|
4.8
|
14.7
|
1.0
|
CB
|
A:ASN364
|
4.9
|
12.6
|
1.0
|
CD2
|
A:TYR167
|
5.0
|
11.8
|
1.0
|
ND1
|
A:HIS323
|
5.0
|
13.0
|
1.0
|
|
Iron binding site 4 out
of 4 in 6hwr
Go back to
Iron Binding Sites List in 6hwr
Iron binding site 4 out
of 4 in the Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Red Kidney Bean Purple Acid Phosphatase in Complex with Adenosine Divanadate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe502
b:23.0
occ:0.78
|
O12
|
D:H1W530
|
1.8
|
22.1
|
0.4
|
OH
|
D:TYR167
|
1.9
|
14.0
|
1.0
|
OD1
|
D:ASP135
|
2.0
|
18.4
|
1.0
|
OD2
|
D:ASP164
|
2.4
|
17.7
|
1.0
|
O10
|
D:H1W530
|
2.4
|
20.7
|
0.4
|
O10
|
D:H1W530
|
2.4
|
22.4
|
0.6
|
NE2
|
D:HIS325
|
2.5
|
19.3
|
1.0
|
V01
|
D:H1W530
|
2.8
|
33.2
|
0.4
|
CG
|
D:ASP135
|
3.0
|
18.3
|
1.0
|
O09
|
D:H1W530
|
3.1
|
27.2
|
0.6
|
CZ
|
D:TYR167
|
3.1
|
15.1
|
1.0
|
CD2
|
D:HIS325
|
3.3
|
17.5
|
1.0
|
CG
|
D:ASP164
|
3.3
|
15.9
|
1.0
|
CB
|
D:ASP135
|
3.3
|
11.3
|
1.0
|
CE1
|
D:HIS325
|
3.5
|
18.4
|
1.0
|
ZN
|
D:ZN501
|
3.6
|
19.1
|
0.8
|
CB
|
D:ASP164
|
3.6
|
10.0
|
1.0
|
CE2
|
D:TYR167
|
3.6
|
12.8
|
1.0
|
V01
|
D:H1W530
|
3.7
|
46.2
|
0.6
|
O09
|
D:H1W530
|
3.9
|
20.1
|
0.4
|
O
|
D:HIS323
|
4.1
|
15.2
|
1.0
|
OD2
|
D:ASP135
|
4.1
|
14.1
|
1.0
|
O11
|
D:H1W530
|
4.2
|
27.7
|
0.4
|
CE1
|
D:TYR167
|
4.2
|
15.1
|
1.0
|
O12
|
D:H1W530
|
4.2
|
29.3
|
0.6
|
CD2
|
D:HIS202
|
4.2
|
17.4
|
1.0
|
CA
|
D:ASP135
|
4.3
|
13.8
|
1.0
|
OD1
|
D:ASP164
|
4.5
|
14.4
|
1.0
|
CA
|
D:HIS323
|
4.5
|
13.4
|
1.0
|
CG
|
D:HIS325
|
4.5
|
18.7
|
1.0
|
O15
|
D:H1W530
|
4.5
|
30.5
|
0.4
|
CE1
|
D:HIS286
|
4.5
|
10.9
|
1.0
|
NE2
|
D:HIS286
|
4.5
|
14.4
|
1.0
|
ND1
|
D:HIS325
|
4.6
|
19.7
|
1.0
|
NE2
|
D:HIS202
|
4.6
|
16.5
|
1.0
|
C
|
D:HIS323
|
4.7
|
17.7
|
1.0
|
CB
|
D:ASP364
|
4.8
|
12.3
|
1.0
|
N
|
D:HIS323
|
4.8
|
12.2
|
1.0
|
O11
|
D:H1W530
|
4.9
|
31.2
|
0.6
|
|
Reference:
D.Feder,
L.R.Gahan,
R.P.Mcgeary,
L.W.Guddat,
G.Schenk.
The Binding Mode of An Adp Analogue to A Metallohydrolase Mimics the Likely Transition State. Chembiochem V. 20 1536 2019.
ISSN: ESSN 1439-7633
PubMed: 30719821
DOI: 10.1002/CBIC.201900077
Page generated: Tue Aug 6 21:53:25 2024
|