Zinc in PDB 2ke1: Molecular Basis of Non-Modified Histone H3 Tail Recognition By the First Phd Finger of Autoimmune Regulator
Zinc Binding Sites:
The binding sites of Zinc atom in the Molecular Basis of Non-Modified Histone H3 Tail Recognition By the First Phd Finger of Autoimmune Regulator
(pdb code 2ke1). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Molecular Basis of Non-Modified Histone H3 Tail Recognition By the First Phd Finger of Autoimmune Regulator, PDB code: 2ke1:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 2ke1
Go back to
Zinc Binding Sites List in 2ke1
Zinc binding site 1 out
of 2 in the Molecular Basis of Non-Modified Histone H3 Tail Recognition By the First Phd Finger of Autoimmune Regulator
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Molecular Basis of Non-Modified Histone H3 Tail Recognition By the First Phd Finger of Autoimmune Regulator within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn355
b:0.2
occ:1.00
|
HB
|
A:VAL301
|
2.2
|
0.2
|
1.0
|
ND1
|
A:HIS319
|
2.5
|
0.2
|
1.0
|
SG
|
A:CYS302
|
2.5
|
0.3
|
1.0
|
SG
|
A:CYS299
|
2.5
|
0.2
|
1.0
|
SG
|
A:CYS322
|
2.6
|
0.2
|
1.0
|
HB2
|
A:HIS319
|
2.6
|
0.1
|
1.0
|
H
|
A:CYS302
|
2.8
|
0.2
|
1.0
|
HB2
|
A:CYS322
|
2.9
|
0.2
|
1.0
|
HB3
|
A:CYS322
|
3.0
|
0.2
|
1.0
|
CB
|
A:CYS322
|
3.0
|
0.2
|
1.0
|
HB3
|
A:CYS299
|
3.1
|
0.2
|
1.0
|
CB
|
A:VAL301
|
3.2
|
0.2
|
1.0
|
H
|
A:HIS319
|
3.3
|
0.1
|
1.0
|
CB
|
A:CYS299
|
3.4
|
0.2
|
1.0
|
CG
|
A:HIS319
|
3.4
|
0.1
|
1.0
|
CB
|
A:HIS319
|
3.5
|
0.1
|
1.0
|
HG11
|
A:VAL301
|
3.6
|
1.0
|
1.0
|
CE1
|
A:HIS319
|
3.6
|
0.2
|
1.0
|
N
|
A:CYS302
|
3.6
|
0.2
|
1.0
|
HG13
|
A:VAL301
|
3.6
|
1.0
|
1.0
|
HB2
|
A:CYS299
|
3.6
|
0.2
|
1.0
|
CG1
|
A:VAL301
|
3.7
|
0.2
|
1.0
|
HE1
|
A:HIS319
|
3.8
|
0.2
|
1.0
|
CB
|
A:CYS302
|
3.9
|
0.3
|
1.0
|
HG22
|
A:VAL301
|
3.9
|
1.0
|
1.0
|
H
|
A:VAL301
|
3.9
|
0.2
|
1.0
|
CG2
|
A:VAL301
|
4.0
|
0.2
|
1.0
|
HB3
|
A:CYS302
|
4.1
|
0.4
|
1.0
|
N
|
A:HIS319
|
4.1
|
0.1
|
1.0
|
HG23
|
A:VAL301
|
4.2
|
1.0
|
1.0
|
CA
|
A:VAL301
|
4.2
|
0.2
|
1.0
|
HB3
|
A:HIS319
|
4.2
|
0.2
|
1.0
|
C
|
A:VAL301
|
4.3
|
0.2
|
1.0
|
HB3
|
A:ASP304
|
4.3
|
0.6
|
1.0
|
CA
|
A:CYS302
|
4.3
|
0.3
|
1.0
|
CA
|
A:HIS319
|
4.4
|
0.1
|
1.0
|
N
|
A:VAL301
|
4.4
|
0.2
|
1.0
|
H
|
A:ASP304
|
4.5
|
0.2
|
1.0
|
CA
|
A:CYS322
|
4.5
|
0.2
|
1.0
|
CD2
|
A:HIS319
|
4.6
|
0.2
|
1.0
|
NE2
|
A:HIS319
|
4.7
|
0.2
|
1.0
|
HG12
|
A:VAL301
|
4.8
|
1.1
|
1.0
|
HB2
|
A:CYS302
|
4.8
|
0.4
|
1.0
|
CA
|
A:CYS299
|
4.8
|
0.2
|
1.0
|
H
|
A:ARG303
|
4.8
|
0.3
|
1.0
|
HA
|
A:PHE318
|
4.8
|
0.1
|
1.0
|
H
|
A:CYS322
|
4.8
|
0.2
|
1.0
|
HA
|
A:CYS322
|
4.9
|
0.2
|
1.0
|
|
Zinc binding site 2 out
of 2 in 2ke1
Go back to
Zinc Binding Sites List in 2ke1
Zinc binding site 2 out
of 2 in the Molecular Basis of Non-Modified Histone H3 Tail Recognition By the First Phd Finger of Autoimmune Regulator
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Molecular Basis of Non-Modified Histone H3 Tail Recognition By the First Phd Finger of Autoimmune Regulator within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn356
b:0.7
occ:1.00
|
HB2
|
A:CYS314
|
1.7
|
1.2
|
1.0
|
SG
|
A:CYS340
|
2.4
|
0.6
|
1.0
|
CB
|
A:CYS314
|
2.4
|
0.3
|
1.0
|
SG
|
A:CYS337
|
2.5
|
0.6
|
1.0
|
SG
|
A:CYS311
|
2.5
|
0.2
|
1.0
|
SG
|
A:CYS314
|
2.5
|
1.3
|
1.0
|
H
|
A:CYS337
|
2.8
|
0.2
|
1.0
|
HB3
|
A:CYS314
|
3.1
|
0.9
|
1.0
|
HB3
|
A:CYS311
|
3.1
|
0.2
|
1.0
|
CB
|
A:CYS311
|
3.2
|
0.2
|
1.0
|
HB2
|
A:CYS311
|
3.3
|
0.2
|
1.0
|
H
|
A:CYS314
|
3.4
|
0.3
|
1.0
|
CA
|
A:CYS314
|
3.6
|
0.2
|
1.0
|
HB3
|
A:CYS337
|
3.6
|
0.5
|
1.0
|
N
|
A:CYS314
|
3.6
|
0.2
|
1.0
|
CB
|
A:CYS337
|
3.7
|
0.4
|
1.0
|
N
|
A:CYS337
|
3.7
|
0.2
|
1.0
|
HB2
|
A:CYS340
|
3.8
|
0.4
|
1.0
|
CB
|
A:CYS340
|
3.9
|
0.5
|
1.0
|
HA
|
A:ARG336
|
4.0
|
0.2
|
1.0
|
H
|
A:CYS340
|
4.2
|
0.5
|
1.0
|
CA
|
A:CYS337
|
4.3
|
0.3
|
1.0
|
HA
|
A:CYS314
|
4.3
|
0.3
|
1.0
|
O
|
A:CYS314
|
4.4
|
0.2
|
1.0
|
C
|
A:CYS314
|
4.4
|
0.2
|
1.0
|
HB3
|
A:CYS340
|
4.5
|
0.5
|
1.0
|
C
|
A:GLY313
|
4.5
|
0.3
|
1.0
|
HB2
|
A:CYS337
|
4.6
|
0.5
|
1.0
|
HB3
|
A:ARG336
|
4.7
|
0.3
|
1.0
|
CA
|
A:CYS311
|
4.7
|
0.1
|
1.0
|
C
|
A:ARG336
|
4.7
|
0.2
|
1.0
|
H
|
A:GLY313
|
4.7
|
0.3
|
1.0
|
CA
|
A:ARG336
|
4.8
|
0.2
|
1.0
|
HB2
|
A:ARG316
|
4.8
|
0.3
|
1.0
|
HG2
|
A:ARG336
|
4.8
|
0.5
|
1.0
|
HB3
|
A:SER339
|
4.8
|
1.2
|
1.0
|
N
|
A:CYS340
|
4.8
|
0.5
|
1.0
|
CA
|
A:CYS340
|
4.9
|
0.5
|
1.0
|
HE1
|
A:PHE318
|
5.0
|
0.2
|
1.0
|
|
Reference:
F.Chignola,
M.Gaetani,
A.Rebane,
T.Org,
L.Mollica,
C.Zucchelli,
A.Spitaleri,
V.Mannella,
P.Peterson,
G.Musco.
The Solution Structure of the First Phd Finger of Autoimmune Regulator in Complex with Non-Modified Histone H3 Tail Reveals the Antagonistic Role of H3R2 Methylation Nucleic Acids Res. V. 37 2951 2009.
ISSN: ISSN 0305-1048
PubMed: 19293276
DOI: 10.1093/NAR/GKP166
Page generated: Thu Oct 17 01:34:30 2024
|