Zinc in PDB 1wxo: Structure of Archaeal Trans-Editing Protein Alax in Complex with Zinc
Protein crystallography data
The structure of Structure of Archaeal Trans-Editing Protein Alax in Complex with Zinc, PDB code: 1wxo
was solved by
M.Sokabe,
A.Okada,
T.Nakashima,
M.Yao,
I.Tanaka,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
1.88
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
42.472,
97.971,
60.584,
90.00,
95.81,
90.00
|
R / Rfree (%)
|
19.3 /
23.2
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Archaeal Trans-Editing Protein Alax in Complex with Zinc
(pdb code 1wxo). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Structure of Archaeal Trans-Editing Protein Alax in Complex with Zinc, PDB code: 1wxo:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 1wxo
Go back to
Zinc Binding Sites List in 1wxo
Zinc binding site 1 out
of 3 in the Structure of Archaeal Trans-Editing Protein Alax in Complex with Zinc
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structure of Archaeal Trans-Editing Protein Alax in Complex with Zinc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1001
b:30.1
occ:1.00
|
NE2
|
A:HIS120
|
2.0
|
19.7
|
1.0
|
NE2
|
A:HIS9
|
2.0
|
30.6
|
1.0
|
NE2
|
A:HIS13
|
2.2
|
19.2
|
1.0
|
SG
|
A:CYS116
|
2.3
|
21.1
|
1.0
|
CE1
|
A:HIS120
|
2.8
|
22.8
|
1.0
|
CD2
|
A:HIS9
|
2.9
|
29.7
|
1.0
|
CE1
|
A:HIS9
|
3.0
|
32.5
|
1.0
|
CD2
|
A:HIS120
|
3.1
|
21.7
|
1.0
|
CE1
|
A:HIS13
|
3.1
|
22.8
|
1.0
|
CD2
|
A:HIS13
|
3.2
|
19.8
|
1.0
|
CB
|
A:CYS116
|
3.3
|
19.9
|
1.0
|
ND1
|
A:HIS120
|
3.9
|
20.0
|
1.0
|
CG
|
A:HIS9
|
4.0
|
29.4
|
1.0
|
ND1
|
A:HIS9
|
4.0
|
29.8
|
1.0
|
CG
|
A:HIS120
|
4.1
|
20.8
|
1.0
|
ND1
|
A:HIS13
|
4.2
|
23.0
|
1.0
|
CG2
|
A:VAL106
|
4.2
|
17.5
|
1.0
|
CG
|
A:HIS13
|
4.3
|
18.9
|
1.0
|
O
|
A:HOH1139
|
4.3
|
43.7
|
1.0
|
CB
|
A:LYS118
|
4.5
|
28.0
|
1.0
|
O
|
A:HIS9
|
4.6
|
18.9
|
1.0
|
CA
|
A:CYS116
|
4.7
|
19.4
|
1.0
|
N
|
A:LYS118
|
4.9
|
25.4
|
1.0
|
O
|
A:LYS118
|
5.0
|
23.4
|
1.0
|
C
|
A:CYS116
|
5.0
|
21.0
|
1.0
|
|
Zinc binding site 2 out
of 3 in 1wxo
Go back to
Zinc Binding Sites List in 1wxo
Zinc binding site 2 out
of 3 in the Structure of Archaeal Trans-Editing Protein Alax in Complex with Zinc
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structure of Archaeal Trans-Editing Protein Alax in Complex with Zinc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1002
b:26.5
occ:1.00
|
NE2
|
B:HIS9
|
1.9
|
21.6
|
1.0
|
NE2
|
B:HIS120
|
1.9
|
23.0
|
1.0
|
NE2
|
B:HIS13
|
2.1
|
21.2
|
1.0
|
SG
|
B:CYS116
|
2.3
|
20.5
|
1.0
|
CE1
|
B:HIS120
|
2.8
|
24.3
|
1.0
|
CE1
|
B:HIS9
|
2.9
|
22.6
|
1.0
|
CD2
|
B:HIS9
|
2.9
|
22.9
|
1.0
|
CE1
|
B:HIS13
|
3.0
|
22.4
|
1.0
|
CD2
|
B:HIS13
|
3.1
|
22.2
|
1.0
|
CD2
|
B:HIS120
|
3.1
|
24.2
|
1.0
|
CB
|
B:CYS116
|
3.3
|
19.5
|
1.0
|
ND1
|
B:HIS120
|
3.9
|
24.1
|
1.0
|
ND1
|
B:HIS9
|
4.0
|
23.0
|
1.0
|
CG
|
B:HIS9
|
4.0
|
22.9
|
1.0
|
CG
|
B:HIS120
|
4.1
|
23.3
|
1.0
|
ND1
|
B:HIS13
|
4.1
|
22.5
|
1.0
|
CG2
|
B:VAL106
|
4.1
|
19.4
|
1.0
|
CG
|
B:HIS13
|
4.2
|
20.4
|
1.0
|
CB
|
B:LYS118
|
4.5
|
26.8
|
1.0
|
CA
|
B:CYS116
|
4.7
|
19.7
|
1.0
|
O
|
B:HIS9
|
4.7
|
18.5
|
1.0
|
O
|
B:HOH1102
|
4.8
|
37.8
|
1.0
|
N
|
B:LYS118
|
4.9
|
26.7
|
1.0
|
CG
|
B:LYS118
|
5.0
|
28.8
|
1.0
|
CB
|
B:VAL106
|
5.0
|
18.8
|
1.0
|
|
Zinc binding site 3 out
of 3 in 1wxo
Go back to
Zinc Binding Sites List in 1wxo
Zinc binding site 3 out
of 3 in the Structure of Archaeal Trans-Editing Protein Alax in Complex with Zinc
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structure of Archaeal Trans-Editing Protein Alax in Complex with Zinc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn1003
b:28.3
occ:1.00
|
NE2
|
C:HIS9
|
1.9
|
31.7
|
1.0
|
NE2
|
C:HIS120
|
2.0
|
26.7
|
1.0
|
NE2
|
C:HIS13
|
2.1
|
20.2
|
1.0
|
SG
|
C:CYS116
|
2.2
|
26.5
|
1.0
|
CE1
|
C:HIS120
|
2.7
|
25.7
|
1.0
|
CE1
|
C:HIS9
|
2.8
|
30.4
|
1.0
|
CD2
|
C:HIS9
|
3.0
|
31.4
|
1.0
|
CE1
|
C:HIS13
|
3.0
|
20.4
|
1.0
|
CD2
|
C:HIS120
|
3.1
|
26.1
|
1.0
|
CD2
|
C:HIS13
|
3.2
|
21.6
|
1.0
|
CB
|
C:CYS116
|
3.3
|
26.4
|
1.0
|
ND1
|
C:HIS120
|
3.9
|
28.0
|
1.0
|
ND1
|
C:HIS9
|
3.9
|
31.5
|
1.0
|
CG
|
C:HIS9
|
4.0
|
31.6
|
1.0
|
CG
|
C:HIS120
|
4.1
|
25.7
|
1.0
|
ND1
|
C:HIS13
|
4.1
|
18.9
|
1.0
|
CG
|
C:HIS13
|
4.2
|
19.7
|
1.0
|
CG2
|
C:VAL106
|
4.3
|
19.5
|
1.0
|
CB
|
C:LYS118
|
4.4
|
35.9
|
1.0
|
CA
|
C:CYS116
|
4.7
|
24.4
|
1.0
|
O
|
C:HIS9
|
4.8
|
22.4
|
1.0
|
N
|
C:LYS118
|
4.9
|
34.2
|
1.0
|
CB
|
C:VAL106
|
5.0
|
20.9
|
1.0
|
O
|
C:LYS118
|
5.0
|
32.6
|
1.0
|
|
Reference:
M.Sokabe,
A.Okada,
M.Yao,
T.Nakashima,
I.Tanaka.
Molecular Basis of Alanine Discrimination in Editing Site Proc.Natl.Acad.Sci.Usa V. 102 11669 2005.
ISSN: ISSN 0027-8424
PubMed: 16087889
DOI: 10.1073/PNAS.0502119102
Page generated: Wed Oct 16 20:12:31 2024
|