Zinc in PDB 2nqh: High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant
Enzymatic activity of High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant
All present enzymatic activity of High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant:
3.1.21.2;
Protein crystallography data
The structure of High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant, PDB code: 2nqh
was solved by
E.D.Garcin-Hosfield,
D.J.Hosfield,
J.A.Tainer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
1.10
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
49.800,
59.200,
50.900,
90.00,
111.00,
90.00
|
R / Rfree (%)
|
15.5 /
19.2
|
Zinc Binding Sites:
The binding sites of Zinc atom in the High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant
(pdb code 2nqh). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant, PDB code: 2nqh:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 2nqh
Go back to
Zinc Binding Sites List in 2nqh
Zinc binding site 1 out
of 3 in the High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:9.2
occ:1.00
|
O2
|
A:PO4999
|
2.0
|
10.7
|
1.0
|
NE2
|
A:HIS109
|
2.0
|
10.3
|
1.0
|
OE2
|
A:GLU145
|
2.0
|
8.0
|
1.0
|
NE2
|
A:HIS69
|
2.0
|
9.6
|
1.0
|
O1
|
A:PO4999
|
2.6
|
14.8
|
1.0
|
P
|
A:PO4999
|
2.9
|
13.1
|
1.0
|
CD2
|
A:HIS109
|
2.9
|
10.5
|
1.0
|
CD
|
A:GLU145
|
2.9
|
7.3
|
1.0
|
CE1
|
A:HIS69
|
3.0
|
9.2
|
1.0
|
CE1
|
A:HIS109
|
3.0
|
12.2
|
1.0
|
CD2
|
A:HIS69
|
3.1
|
7.8
|
1.0
|
OE1
|
A:GLU145
|
3.1
|
7.7
|
1.0
|
ZN
|
A:ZN302
|
3.5
|
8.8
|
1.0
|
O3
|
A:PO4999
|
3.8
|
11.7
|
1.0
|
O4
|
A:PO4999
|
4.0
|
14.1
|
1.0
|
OD1
|
A:ASN107
|
4.0
|
10.2
|
1.0
|
CG
|
A:HIS109
|
4.1
|
9.8
|
1.0
|
ND1
|
A:HIS109
|
4.1
|
11.6
|
1.0
|
ND1
|
A:HIS69
|
4.2
|
9.7
|
1.0
|
CE1
|
A:HIS216
|
4.2
|
6.5
|
1.0
|
NE2
|
A:GLN261
|
4.2
|
7.2
|
1.0
|
CG
|
A:HIS69
|
4.2
|
7.7
|
1.0
|
CG
|
A:GLU145
|
4.3
|
8.2
|
1.0
|
ND1
|
A:HIS216
|
4.3
|
6.6
|
1.0
|
CE1
|
A:HIS182
|
4.4
|
7.2
|
1.0
|
CB
|
A:GLU145
|
4.7
|
7.8
|
1.0
|
OE1
|
A:GLN261
|
4.9
|
6.7
|
1.0
|
CD
|
A:GLN261
|
5.0
|
7.1
|
1.0
|
|
Zinc binding site 2 out
of 3 in 2nqh
Go back to
Zinc Binding Sites List in 2nqh
Zinc binding site 2 out
of 3 in the High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn302
b:8.8
occ:1.00
|
O2
|
A:PO4999
|
2.1
|
10.7
|
1.0
|
OD1
|
A:ASP179
|
2.1
|
7.3
|
1.0
|
OE1
|
A:GLU145
|
2.2
|
7.7
|
1.0
|
OE1
|
A:GLN261
|
2.2
|
6.7
|
1.0
|
ND1
|
A:HIS216
|
2.2
|
6.6
|
1.0
|
CD
|
A:GLN261
|
3.0
|
7.1
|
1.0
|
CD
|
A:GLU145
|
3.1
|
7.3
|
1.0
|
NE2
|
A:GLN261
|
3.1
|
7.2
|
1.0
|
CE1
|
A:HIS216
|
3.1
|
6.5
|
1.0
|
CG
|
A:ASP179
|
3.2
|
7.0
|
1.0
|
CG
|
A:HIS216
|
3.2
|
6.3
|
1.0
|
P
|
A:PO4999
|
3.4
|
13.1
|
1.0
|
OE2
|
A:GLU145
|
3.4
|
8.0
|
1.0
|
ZN
|
A:ZN301
|
3.5
|
9.2
|
1.0
|
CB
|
A:HIS216
|
3.5
|
6.4
|
1.0
|
CB
|
A:ASP179
|
3.7
|
6.9
|
1.0
|
CE1
|
A:HIS182
|
3.7
|
7.2
|
1.0
|
O4
|
A:PO4999
|
3.9
|
14.1
|
1.0
|
O3
|
A:PO4999
|
3.9
|
11.7
|
1.0
|
ND2
|
A:ASN218
|
4.1
|
7.7
|
1.0
|
NE2
|
A:HIS182
|
4.1
|
7.3
|
1.0
|
OD2
|
A:ASP179
|
4.3
|
7.3
|
1.0
|
NE2
|
A:HIS216
|
4.3
|
7.2
|
1.0
|
ND1
|
A:HIS182
|
4.3
|
6.8
|
1.0
|
CG
|
A:GLU145
|
4.3
|
8.2
|
1.0
|
CD2
|
A:HIS216
|
4.3
|
6.6
|
1.0
|
CG
|
A:GLN261
|
4.4
|
8.0
|
1.0
|
O1
|
A:PO4999
|
4.5
|
14.8
|
1.0
|
ZN
|
A:ZN303
|
4.6
|
8.9
|
1.0
|
CE1
|
A:HIS231
|
4.6
|
9.4
|
1.0
|
NE2
|
A:HIS109
|
4.8
|
10.3
|
1.0
|
NE2
|
A:HIS231
|
4.8
|
8.3
|
1.0
|
CA
|
A:ASP179
|
4.9
|
7.2
|
1.0
|
NE2
|
A:HIS69
|
4.9
|
9.6
|
1.0
|
CD2
|
A:HIS182
|
5.0
|
7.4
|
1.0
|
|
Zinc binding site 3 out
of 3 in 2nqh
Go back to
Zinc Binding Sites List in 2nqh
Zinc binding site 3 out
of 3 in the High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of High Resolution Crystal Structure of Escherichia Coli Endonuclease IV (Endo IV) E261Q Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn303
b:8.9
occ:1.00
|
OD1
|
A:ASP229
|
2.0
|
21.3
|
1.0
|
NE2
|
A:HIS182
|
2.0
|
7.3
|
1.0
|
O3
|
A:PO4999
|
2.0
|
11.7
|
1.0
|
NE2
|
A:HIS231
|
2.0
|
8.3
|
1.0
|
OD2
|
A:ASP229
|
2.6
|
16.2
|
1.0
|
CG
|
A:ASP229
|
2.6
|
13.9
|
1.0
|
CE1
|
A:HIS182
|
3.0
|
7.2
|
1.0
|
CE1
|
A:HIS231
|
3.0
|
9.4
|
1.0
|
CD2
|
A:HIS231
|
3.1
|
8.4
|
1.0
|
CD2
|
A:HIS182
|
3.1
|
7.4
|
1.0
|
P
|
A:PO4999
|
3.3
|
13.1
|
1.0
|
O4
|
A:PO4999
|
3.9
|
14.1
|
1.0
|
O2
|
A:PO4999
|
4.0
|
10.7
|
1.0
|
CB
|
A:ASP229
|
4.1
|
12.9
|
1.0
|
ND1
|
A:HIS231
|
4.1
|
8.4
|
1.0
|
OD1
|
A:ASP179
|
4.1
|
7.3
|
1.0
|
ND1
|
A:HIS182
|
4.2
|
6.8
|
1.0
|
CG
|
A:HIS231
|
4.2
|
7.8
|
1.0
|
CG
|
A:HIS182
|
4.2
|
7.1
|
1.0
|
O
|
A:HOH1247
|
4.4
|
50.0
|
1.0
|
O1
|
A:PO4999
|
4.4
|
14.8
|
1.0
|
O
|
A:HOH1121
|
4.5
|
34.1
|
1.0
|
ZN
|
A:ZN302
|
4.6
|
8.8
|
1.0
|
O
|
A:HOH1033
|
4.7
|
13.8
|
1.0
|
CG
|
A:ASP179
|
4.9
|
7.0
|
1.0
|
OE1
|
A:GLN261
|
4.9
|
6.7
|
1.0
|
CA
|
A:ASP229
|
5.0
|
11.0
|
1.0
|
|
Reference:
E.D.Garcin,
D.J.Hosfield,
S.A.Desai,
B.J.Haas,
M.Bjoras,
R.P.Cunningham,
J.A.Tainer.
Dna Apurinic-Apyrimidinic Site Binding and Excision By Endonuclease IV. Nat.Struct.Mol.Biol. V. 15 515 2008.
ISSN: ISSN 1545-9993
PubMed: 18408731
DOI: 10.1038/NSMB.1414
Page generated: Thu Oct 17 02:15:41 2024
|