Zinc in PDB 1ef0: Crystal Structure of Pi-Scei Miniprecursor
Enzymatic activity of Crystal Structure of Pi-Scei Miniprecursor
All present enzymatic activity of Crystal Structure of Pi-Scei Miniprecursor:
3.6.1.34;
Protein crystallography data
The structure of Crystal Structure of Pi-Scei Miniprecursor, PDB code: 1ef0
was solved by
B.W.Poland,
M.-Q.Xu,
F.A.Quiocho,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
2.10
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
59.003,
101.683,
86.765,
90.00,
93.51,
90.00
|
R / Rfree (%)
|
23.1 /
28.1
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Pi-Scei Miniprecursor
(pdb code 1ef0). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Crystal Structure of Pi-Scei Miniprecursor, PDB code: 1ef0:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 1ef0
Go back to
Zinc Binding Sites List in 1ef0
Zinc binding site 1 out
of 3 in the Crystal Structure of Pi-Scei Miniprecursor
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 Pi-Scei Miniprecursor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn701
b:13.4
occ:0.25
|
ZN
|
A:ZN701
|
0.0
|
13.4
|
0.2
|
SG
|
A:CYS455
|
1.8
|
28.8
|
0.2
|
O
|
A:HOH875
|
2.1
|
34.9
|
0.2
|
ND1
|
A:HIS442
|
2.3
|
30.8
|
0.2
|
ND1
|
A:HIS442
|
2.4
|
30.5
|
0.5
|
NE2
|
A:HIS453
|
2.4
|
24.0
|
0.2
|
ZN
|
A:ZN701
|
2.4
|
42.7
|
0.2
|
CE1
|
A:HIS453
|
2.4
|
23.5
|
0.5
|
CE1
|
A:HIS453
|
2.5
|
23.9
|
0.2
|
NE2
|
A:HIS453
|
2.6
|
23.3
|
0.5
|
CE1
|
A:HIS442
|
3.3
|
31.0
|
0.2
|
CG
|
A:HIS442
|
3.3
|
30.8
|
0.2
|
CE1
|
A:HIS442
|
3.4
|
30.8
|
0.5
|
CG
|
A:HIS442
|
3.4
|
30.4
|
0.5
|
CB
|
A:HIS442
|
3.6
|
30.6
|
0.2
|
CB
|
A:HIS442
|
3.6
|
30.3
|
0.5
|
CB
|
A:CYS455
|
3.6
|
28.6
|
0.2
|
ND1
|
A:HIS453
|
3.7
|
23.7
|
0.5
|
CD2
|
A:HIS453
|
3.8
|
23.9
|
0.2
|
ND1
|
A:HIS453
|
3.8
|
23.9
|
0.2
|
CD2
|
A:HIS453
|
4.0
|
23.5
|
0.5
|
NE2
|
A:HIS442
|
4.5
|
30.9
|
0.2
|
OE1
|
A:GLU80
|
4.5
|
18.8
|
0.2
|
CG
|
A:HIS453
|
4.5
|
24.0
|
0.2
|
CD2
|
A:HIS442
|
4.5
|
30.8
|
0.2
|
NE2
|
A:HIS442
|
4.5
|
30.6
|
0.5
|
CG
|
A:HIS453
|
4.5
|
23.6
|
0.5
|
CD2
|
A:HIS442
|
4.5
|
30.4
|
0.5
|
O
|
A:ALA454
|
4.5
|
28.2
|
1.0
|
SG
|
A:CYS455
|
4.5
|
30.8
|
0.5
|
CA
|
A:CYS455
|
4.6
|
29.1
|
0.5
|
OE1
|
A:GLU80
|
4.6
|
22.0
|
0.5
|
CA
|
A:CYS455
|
4.6
|
28.6
|
0.2
|
|
Zinc binding site 2 out
of 3 in 1ef0
Go back to
Zinc Binding Sites List in 1ef0
Zinc binding site 2 out
of 3 in the Crystal Structure of Pi-Scei Miniprecursor
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 Pi-Scei Miniprecursor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn701
b:42.7
occ:0.25
|
ZN
|
A:ZN701
|
0.0
|
42.7
|
0.2
|
SG
|
A:CYS455
|
2.4
|
28.8
|
0.2
|
NE2
|
A:HIS453
|
2.4
|
23.3
|
0.5
|
ZN
|
A:ZN701
|
2.4
|
13.4
|
0.2
|
OE1
|
A:GLU80
|
2.5
|
22.0
|
0.5
|
OE1
|
A:GLU80
|
2.8
|
18.8
|
0.2
|
CE1
|
A:HIS453
|
2.8
|
23.9
|
0.2
|
SG
|
A:CYS455
|
3.1
|
30.8
|
0.5
|
O
|
A:HOH875
|
3.2
|
19.4
|
0.5
|
NE2
|
A:HIS453
|
3.2
|
24.0
|
0.2
|
CB
|
A:CYS455
|
3.2
|
28.6
|
0.2
|
CE1
|
A:HIS453
|
3.3
|
23.5
|
0.5
|
CD2
|
A:HIS453
|
3.5
|
23.5
|
0.5
|
CD
|
A:GLU80
|
3.6
|
21.1
|
0.5
|
CD
|
A:GLU80
|
3.7
|
19.0
|
0.2
|
ND1
|
A:HIS453
|
3.8
|
23.9
|
0.2
|
O
|
A:HOH875
|
3.8
|
34.9
|
0.2
|
OE2
|
A:GLU80
|
3.9
|
21.4
|
0.5
|
OE2
|
A:GLU80
|
4.3
|
19.0
|
0.2
|
CD2
|
A:HIS453
|
4.3
|
23.9
|
0.2
|
CB
|
A:CYS455
|
4.4
|
29.2
|
0.5
|
ND1
|
A:HIS453
|
4.5
|
23.7
|
0.5
|
CG
|
A:HIS453
|
4.6
|
23.6
|
0.5
|
CG
|
A:HIS453
|
4.6
|
24.0
|
0.2
|
ND1
|
A:HIS442
|
4.6
|
30.8
|
0.2
|
CA
|
A:CYS455
|
4.6
|
29.1
|
0.5
|
CG
|
A:GLU80
|
4.7
|
19.2
|
0.2
|
CA
|
A:CYS455
|
4.7
|
28.6
|
0.2
|
ND1
|
A:HIS442
|
4.7
|
30.5
|
0.5
|
CG
|
A:GLU80
|
4.9
|
20.8
|
0.5
|
|
Zinc binding site 3 out
of 3 in 1ef0
Go back to
Zinc Binding Sites List in 1ef0
Zinc binding site 3 out
of 3 in the Crystal Structure of Pi-Scei Miniprecursor
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 Pi-Scei Miniprecursor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn701
b:18.6
occ:1.00
|
OE2
|
B:GLU80
|
2.2
|
23.3
|
1.0
|
O
|
B:HOH719
|
2.4
|
13.7
|
1.0
|
NE2
|
B:HIS453
|
2.5
|
19.3
|
1.0
|
SG
|
B:CYS455
|
2.5
|
29.3
|
1.0
|
CD
|
B:GLU80
|
3.0
|
22.5
|
1.0
|
OE1
|
B:GLU80
|
3.1
|
23.6
|
1.0
|
CD2
|
B:HIS453
|
3.3
|
18.4
|
1.0
|
CB
|
B:CYS455
|
3.5
|
26.7
|
1.0
|
CE1
|
B:HIS453
|
3.5
|
19.2
|
1.0
|
CA
|
B:CYS455
|
3.7
|
27.1
|
1.0
|
O
|
B:HOH841
|
4.0
|
35.6
|
1.0
|
N
|
B:CYS455
|
4.1
|
25.1
|
1.0
|
CG
|
B:GLU80
|
4.3
|
21.3
|
1.0
|
CG
|
B:HIS453
|
4.5
|
19.2
|
1.0
|
ND1
|
B:HIS453
|
4.6
|
18.7
|
1.0
|
C
|
B:ALA454
|
4.9
|
23.9
|
1.0
|
CB
|
B:GLU80
|
5.0
|
18.8
|
1.0
|
|
Reference:
B.W.Poland,
M.Q.Xu,
F.A.Quiocho.
Structural Insights Into the Protein Splicing Mechanism of Pi-Scei. J.Biol.Chem. V. 275 16408 2000.
ISSN: ISSN 0021-9258
PubMed: 10828056
DOI: 10.1074/JBC.275.22.16408
Page generated: Sun Oct 13 00:11:01 2024
|