Manganese in PDB 1ecc: Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine
Enzymatic activity of Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine
All present enzymatic activity of Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine:
2.4.2.14;
Protein crystallography data
The structure of Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine, PDB code: 1ecc
was solved by
J.M.Krahn,
J.L.Smith,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
25.00 /
2.40
|
Space group
|
P 43 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
78.200,
78.200,
308.800,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.6 /
26.5
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine
(pdb code 1ecc). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 5 binding sites of Manganese where determined in the
Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine, PDB code: 1ecc:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
Manganese binding site 1 out
of 5 in 1ecc
Go back to
Manganese Binding Sites List in 1ecc
Manganese binding site 1 out
of 5 in the Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn506
b:37.2
occ:1.00
|
O2
|
A:PCP505
|
2.1
|
33.2
|
1.0
|
O3
|
A:PCP505
|
2.1
|
33.7
|
1.0
|
O1
|
A:PCP505
|
2.2
|
35.2
|
1.0
|
O
|
A:HOH2378
|
2.2
|
31.6
|
1.0
|
O1B
|
A:PCP505
|
2.2
|
33.4
|
1.0
|
O
|
A:HOH2379
|
2.2
|
33.6
|
1.0
|
C2
|
A:PCP505
|
2.8
|
33.1
|
1.0
|
C1
|
A:PCP505
|
2.9
|
33.5
|
1.0
|
C3
|
A:PCP505
|
3.0
|
33.1
|
1.0
|
PB
|
A:PCP505
|
3.3
|
37.5
|
1.0
|
OD1
|
A:ASP367
|
3.4
|
40.2
|
1.0
|
O3A
|
A:PCP505
|
3.5
|
37.6
|
1.0
|
PA
|
A:PCP505
|
3.5
|
35.5
|
1.0
|
OD1
|
A:ASP366
|
3.6
|
27.3
|
1.0
|
O
|
A:HOH2411
|
3.7
|
39.1
|
1.0
|
C5
|
A:PCP505
|
3.8
|
32.3
|
1.0
|
O
|
A:PRO302
|
4.0
|
29.1
|
1.0
|
C4
|
A:PCP505
|
4.0
|
33.3
|
1.0
|
O
|
A:ILE301
|
4.2
|
25.7
|
1.0
|
O2B
|
A:PCP505
|
4.2
|
34.9
|
1.0
|
O1A
|
A:PCP505
|
4.3
|
33.8
|
1.0
|
OD2
|
A:ASP366
|
4.4
|
26.4
|
1.0
|
O3B
|
A:PCP505
|
4.4
|
36.8
|
1.0
|
N
|
A:GLU303
|
4.4
|
29.4
|
1.0
|
CG
|
A:ASP366
|
4.4
|
28.2
|
1.0
|
CG
|
A:ASP367
|
4.4
|
39.1
|
1.0
|
O2A
|
A:PCP505
|
4.4
|
36.8
|
1.0
|
C
|
A:PRO302
|
4.5
|
28.9
|
1.0
|
N
|
A:THR304
|
4.5
|
31.2
|
1.0
|
CB
|
A:THR304
|
4.6
|
27.6
|
1.0
|
CE1
|
A:TYR258
|
4.6
|
27.5
|
1.0
|
OG1
|
A:THR304
|
4.6
|
24.3
|
1.0
|
OD2
|
A:ASP367
|
4.7
|
37.7
|
1.0
|
CG2
|
A:ILE301
|
4.9
|
21.3
|
1.0
|
|
Manganese binding site 2 out
of 5 in 1ecc
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Manganese Binding Sites List in 1ecc
Manganese binding site 2 out
of 5 in the Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn2376
b:42.4
occ:0.40
|
OE2
|
A:GLU449
|
2.6
|
44.4
|
1.0
|
CD
|
A:GLU449
|
3.2
|
44.8
|
1.0
|
OE1
|
A:GLU449
|
3.3
|
45.0
|
1.0
|
O
|
A:ALA448
|
4.1
|
36.8
|
1.0
|
ND2
|
A:ASN277
|
4.5
|
23.2
|
1.0
|
CG
|
A:GLU449
|
4.6
|
42.4
|
1.0
|
C
|
A:ALA448
|
4.7
|
37.4
|
1.0
|
OD1
|
A:ASN277
|
4.7
|
24.2
|
1.0
|
CB
|
A:ALA448
|
4.8
|
37.5
|
1.0
|
|
Manganese binding site 3 out
of 5 in 1ecc
Go back to
Manganese Binding Sites List in 1ecc
Manganese binding site 3 out
of 5 in the Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn506
b:32.7
occ:1.00
|
O3
|
B:PCP505
|
2.2
|
29.8
|
1.0
|
O2
|
B:PCP505
|
2.2
|
30.4
|
1.0
|
O1B
|
B:PCP505
|
2.2
|
32.8
|
1.0
|
O
|
B:HOH2452
|
2.3
|
30.3
|
1.0
|
O1
|
B:PCP505
|
2.3
|
32.5
|
1.0
|
O
|
B:HOH2451
|
2.4
|
29.2
|
1.0
|
C2
|
B:PCP505
|
2.9
|
31.7
|
1.0
|
C3
|
B:PCP505
|
3.0
|
30.9
|
1.0
|
C1
|
B:PCP505
|
3.1
|
30.6
|
1.0
|
PB
|
B:PCP505
|
3.4
|
37.8
|
1.0
|
OD1
|
B:ASP367
|
3.4
|
27.4
|
1.0
|
PA
|
B:PCP505
|
3.5
|
34.9
|
1.0
|
O3A
|
B:PCP505
|
3.5
|
35.4
|
1.0
|
OD1
|
B:ASP366
|
3.5
|
22.0
|
1.0
|
O
|
B:HOH2460
|
3.8
|
19.6
|
1.0
|
C5
|
B:PCP505
|
3.9
|
30.3
|
1.0
|
C4
|
B:PCP505
|
4.0
|
30.9
|
1.0
|
OD2
|
B:ASP366
|
4.0
|
15.3
|
1.0
|
O
|
B:PRO302
|
4.1
|
26.3
|
1.0
|
OG1
|
B:THR304
|
4.1
|
26.1
|
1.0
|
O
|
B:ILE301
|
4.2
|
26.9
|
1.0
|
CG
|
B:ASP366
|
4.2
|
16.8
|
1.0
|
O1A
|
B:PCP505
|
4.2
|
33.4
|
1.0
|
CB
|
B:THR304
|
4.3
|
23.0
|
1.0
|
O2B
|
B:PCP505
|
4.3
|
35.4
|
1.0
|
N
|
B:GLU303
|
4.5
|
29.1
|
1.0
|
O3B
|
B:PCP505
|
4.5
|
34.1
|
1.0
|
O2A
|
B:PCP505
|
4.5
|
34.1
|
1.0
|
C
|
B:PRO302
|
4.5
|
27.3
|
1.0
|
N
|
B:THR304
|
4.6
|
24.4
|
1.0
|
CG
|
B:ASP367
|
4.6
|
25.7
|
1.0
|
CE1
|
B:TYR258
|
4.7
|
18.8
|
1.0
|
CG2
|
B:ILE301
|
4.9
|
17.6
|
1.0
|
OD2
|
B:ASP367
|
4.9
|
24.8
|
1.0
|
CD1
|
B:TYR258
|
5.0
|
18.9
|
1.0
|
CA
|
B:THR304
|
5.0
|
23.5
|
1.0
|
|
Manganese binding site 4 out
of 5 in 1ecc
Go back to
Manganese Binding Sites List in 1ecc
Manganese binding site 4 out
of 5 in the Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn1449
b:76.5
occ:0.40
|
O
|
B:ILE428
|
2.8
|
41.1
|
1.0
|
OE2
|
B:GLU376
|
3.0
|
62.9
|
1.0
|
CD
|
B:GLU376
|
3.9
|
64.5
|
1.0
|
C
|
B:ILE428
|
4.0
|
37.8
|
1.0
|
CG
|
B:GLU376
|
4.2
|
58.6
|
1.0
|
C
|
B:ILE429
|
4.7
|
37.5
|
1.0
|
OE2
|
B:GLU380
|
4.7
|
44.8
|
1.0
|
CA
|
B:ILE429
|
4.8
|
36.6
|
1.0
|
O
|
B:ILE429
|
4.9
|
40.9
|
1.0
|
N
|
B:ILE429
|
4.9
|
38.0
|
1.0
|
|
Manganese binding site 5 out
of 5 in 1ecc
Go back to
Manganese Binding Sites List in 1ecc
Manganese binding site 5 out
of 5 in the Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Escherichia Coli Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase Complexed with Mn-Cprpp and 5-Oxo- Norleucine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn2449
b:32.3
occ:1.00
|
OE2
|
B:GLU449
|
2.2
|
31.4
|
1.0
|
O
|
B:HOH2543
|
2.4
|
33.6
|
1.0
|
O
|
B:HOH2597
|
2.4
|
33.5
|
1.0
|
O
|
B:HOH2600
|
2.6
|
32.2
|
1.0
|
O
|
B:HOH2598
|
2.7
|
33.3
|
1.0
|
O
|
B:HOH2599
|
2.7
|
31.7
|
1.0
|
CD
|
B:GLU449
|
3.2
|
32.5
|
1.0
|
OE1
|
B:GLU449
|
3.4
|
33.7
|
1.0
|
OD1
|
B:ASN277
|
3.8
|
19.4
|
1.0
|
ND2
|
B:ASN277
|
4.1
|
19.9
|
1.0
|
CG
|
B:ASN277
|
4.4
|
22.2
|
1.0
|
CB
|
B:SER273
|
4.4
|
21.8
|
1.0
|
CG
|
B:GLU449
|
4.6
|
29.1
|
1.0
|
OG
|
B:SER273
|
4.8
|
24.4
|
1.0
|
O
|
B:HOH2497
|
5.0
|
22.0
|
1.0
|
|
Reference:
J.M.Krahn,
J.H.Kim,
M.R.Burns,
R.J.Parry,
H.Zalkin,
J.L.Smith.
Coupled Formation of An Amidotransferase Interdomain Ammonia Channel and A Phosphoribosyltransferase Active Site. Biochemistry V. 36 11061 1997.
ISSN: ISSN 0006-2960
PubMed: 9333323
DOI: 10.1021/BI9714114
Page generated: Sat Oct 5 10:09:42 2024
|