Zinc in PDB 8ytg: Crystal Structures of Human IRF2BP2 Ring Domain in Complex with IRF2 Peptide
Protein crystallography data
The structure of Crystal Structures of Human IRF2BP2 Ring Domain in Complex with IRF2 Peptide, PDB code: 8ytg
was solved by
G.C.Wang,
J.P.Ding,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
34.43 /
1.45
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
26.733,
39.868,
36.247,
90,
108.21,
90
|
R / Rfree (%)
|
16.5 /
18.9
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structures of Human IRF2BP2 Ring Domain in Complex with IRF2 Peptide
(pdb code 8ytg). 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 Structures of Human IRF2BP2 Ring Domain in Complex with IRF2 Peptide, PDB code: 8ytg:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 8ytg
Go back to
Zinc Binding Sites List in 8ytg
Zinc binding site 1 out
of 3 in the Crystal Structures of Human IRF2BP2 Ring Domain in Complex with IRF2 Peptide
![](/pictures/ZN/pdb/yt/8ytg-ZN-sphere_01.jpg) Mono view
![](/pictures/ZN/pdb/yt/8ytg-ZN-sphere_01_stereo.jpg) Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structures of Human IRF2BP2 Ring Domain in Complex with IRF2 Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn601
b:10.6
occ:1.00
|
SG
|
A:CYS533
|
2.3
|
11.1
|
1.0
|
SG
|
A:CYS509
|
2.3
|
10.9
|
1.0
|
SG
|
A:CYS530
|
2.3
|
10.3
|
1.0
|
SG
|
A:CYS506
|
2.3
|
8.9
|
1.0
|
CB
|
A:CYS533
|
3.2
|
8.6
|
1.0
|
CB
|
A:CYS506
|
3.2
|
8.6
|
1.0
|
CB
|
A:CYS509
|
3.3
|
12.9
|
1.0
|
CB
|
A:CYS530
|
3.5
|
10.7
|
1.0
|
N
|
A:CYS509
|
3.7
|
9.8
|
1.0
|
O
|
A:HOH840
|
3.8
|
31.2
|
1.0
|
N
|
A:CYS530
|
4.0
|
7.7
|
1.0
|
CA
|
A:CYS509
|
4.0
|
11.4
|
1.0
|
N
|
A:CYS533
|
4.3
|
10.5
|
1.0
|
CA
|
A:CYS533
|
4.3
|
11.4
|
1.0
|
CA
|
A:CYS530
|
4.3
|
8.8
|
1.0
|
O
|
A:HOH839
|
4.6
|
22.3
|
1.0
|
CA
|
A:CYS506
|
4.7
|
8.1
|
1.0
|
C
|
A:CYS509
|
4.8
|
12.2
|
1.0
|
CB
|
A:LEU508
|
4.8
|
12.8
|
1.0
|
C
|
A:LEU508
|
4.8
|
12.8
|
1.0
|
O
|
A:CYS530
|
4.9
|
9.3
|
1.0
|
C
|
A:CYS530
|
4.9
|
9.2
|
1.0
|
N
|
A:HIS510
|
4.9
|
10.1
|
1.0
|
|
Zinc binding site 2 out
of 3 in 8ytg
Go back to
Zinc Binding Sites List in 8ytg
Zinc binding site 2 out
of 3 in the Crystal Structures of Human IRF2BP2 Ring Domain in Complex with IRF2 Peptide
![](/pictures/ZN/pdb/yt/8ytg-ZN-sphere_02.jpg) Mono view
![](/pictures/ZN/pdb/yt/8ytg-ZN-sphere_02_stereo.jpg) Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structures of Human IRF2BP2 Ring Domain in Complex with IRF2 Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn602
b:7.0
occ:1.00
|
ND1
|
A:HIS527
|
2.1
|
7.2
|
1.0
|
SG
|
A:CYS555
|
2.3
|
7.5
|
1.0
|
SG
|
A:CYS521
|
2.3
|
5.7
|
1.0
|
SG
|
A:CYS549
|
2.4
|
5.9
|
1.0
|
CE1
|
A:HIS527
|
3.0
|
8.4
|
1.0
|
CG
|
A:HIS527
|
3.1
|
6.5
|
1.0
|
CB
|
A:CYS555
|
3.2
|
8.6
|
1.0
|
CB
|
A:CYS521
|
3.2
|
6.3
|
1.0
|
CB
|
A:CYS549
|
3.3
|
8.8
|
1.0
|
CB
|
A:HIS527
|
3.5
|
7.0
|
1.0
|
OG
|
A:SER551
|
3.6
|
7.4
|
1.0
|
CB
|
A:VAL524
|
4.1
|
7.5
|
1.0
|
CG2
|
A:VAL524
|
4.1
|
8.8
|
1.0
|
NE2
|
A:HIS527
|
4.2
|
9.8
|
1.0
|
NE1
|
A:TRP564
|
4.2
|
7.1
|
1.0
|
CD2
|
A:HIS527
|
4.2
|
8.7
|
1.0
|
CB
|
A:SER551
|
4.4
|
8.2
|
1.0
|
CA
|
A:CYS555
|
4.6
|
7.0
|
1.0
|
CA
|
A:CYS521
|
4.6
|
5.9
|
1.0
|
N
|
A:CYS555
|
4.7
|
7.5
|
1.0
|
CA
|
A:CYS549
|
4.8
|
8.0
|
1.0
|
CG1
|
A:VAL524
|
4.9
|
7.8
|
1.0
|
|
Zinc binding site 3 out
of 3 in 8ytg
Go back to
Zinc Binding Sites List in 8ytg
Zinc binding site 3 out
of 3 in the Crystal Structures of Human IRF2BP2 Ring Domain in Complex with IRF2 Peptide
![](/pictures/ZN/pdb/yt/8ytg-ZN-sphere_03.jpg) Mono view
![](/pictures/ZN/pdb/yt/8ytg-ZN-sphere_03_stereo.jpg) Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structures of Human IRF2BP2 Ring Domain in Complex with IRF2 Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn603
b:18.4
occ:1.00
|
NE
|
B:ARG1
|
3.2
|
7.7
|
1.0
|
N
|
A:ALA565
|
3.3
|
6.5
|
1.0
|
O
|
B:HOH115
|
3.3
|
16.5
|
1.0
|
O
|
A:ALA565
|
3.4
|
8.1
|
1.0
|
O
|
A:HOH781
|
3.4
|
18.2
|
1.0
|
CD2
|
A:LEU557
|
3.6
|
13.0
|
1.0
|
CA
|
A:TRP564
|
3.7
|
6.1
|
1.0
|
NH2
|
B:ARG1
|
3.8
|
9.0
|
1.0
|
CB
|
A:TRP564
|
3.9
|
8.5
|
1.0
|
CZ
|
B:ARG1
|
3.9
|
6.8
|
1.0
|
C
|
A:TRP564
|
4.0
|
6.9
|
1.0
|
CE
|
A:MET567
|
4.0
|
8.8
|
1.0
|
CD
|
B:ARG1
|
4.1
|
10.8
|
1.0
|
CG
|
A:LEU557
|
4.1
|
12.8
|
1.0
|
C
|
A:ALA565
|
4.2
|
7.8
|
1.0
|
CD1
|
A:LEU557
|
4.3
|
17.2
|
1.0
|
CA
|
A:ALA565
|
4.3
|
6.8
|
1.0
|
CG
|
B:ARG1
|
4.6
|
13.2
|
1.0
|
CB
|
A:ALA565
|
4.9
|
7.3
|
1.0
|
O
|
A:PRO563
|
5.0
|
10.3
|
1.0
|
N
|
A:TRP564
|
5.0
|
7.8
|
1.0
|
|
Reference:
G.C.Wang,
J.P.Ding.
IRF2BP2 Recognizes and Bind to A Conserved Rxsvi Sequence Motif of Protein Partners and Interacts with ZBTB16 to Regulate Megakaryocytic Differentiation To Be Published.
Page generated: Wed Nov 27 21:08:10 2024
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