Zinc in PDB 2lgk: uc(Nmr) Structure of UHRF1 Phd Domains in A Complex with Histone H3 Peptide
Zinc Binding Sites:
The binding sites of Zinc atom in the uc(Nmr) Structure of UHRF1 Phd Domains in A Complex with Histone H3 Peptide
(pdb code 2lgk). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
uc(Nmr) Structure of UHRF1 Phd Domains in A Complex with Histone H3 Peptide, PDB code: 2lgk:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 2lgk
Go back to
Zinc Binding Sites List in 2lgk
Zinc binding site 1 out
of 3 in the uc(Nmr) Structure of UHRF1 Phd Domains in A Complex with Histone H3 Peptide
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of uc(Nmr) Structure of UHRF1 Phd Domains in A Complex with Histone H3 Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn380
b:0.0
occ:1.00
|
SG
|
A:CYS329
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS315
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS318
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS326
|
2.3
|
0.0
|
1.0
|
H
|
A:CYS329
|
2.9
|
0.0
|
1.0
|
HB
|
A:VAL328
|
3.0
|
0.0
|
1.0
|
HB3
|
A:CYS326
|
3.1
|
0.0
|
1.0
|
HB3
|
A:CYS318
|
3.2
|
0.0
|
1.0
|
HB3
|
A:CYS329
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS315
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS326
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS329
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS315
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS318
|
3.4
|
0.0
|
1.0
|
N
|
A:CYS329
|
3.4
|
0.0
|
1.0
|
HB2
|
A:CYS315
|
3.4
|
0.0
|
1.0
|
HB2
|
A:CYS326
|
3.9
|
0.0
|
1.0
|
CA
|
A:CYS329
|
4.0
|
0.0
|
1.0
|
HB2
|
A:CYS318
|
4.0
|
0.0
|
1.0
|
CB
|
A:VAL328
|
4.0
|
0.0
|
1.0
|
HG12
|
A:VAL328
|
4.2
|
0.0
|
1.0
|
H
|
A:CYS318
|
4.2
|
0.0
|
1.0
|
HB2
|
A:CYS329
|
4.2
|
0.0
|
1.0
|
C
|
A:VAL328
|
4.3
|
0.0
|
1.0
|
H
|
A:VAL328
|
4.4
|
0.0
|
1.0
|
O
|
A:CYS326
|
4.4
|
0.0
|
1.0
|
CA
|
A:CYS326
|
4.5
|
0.0
|
1.0
|
CA
|
A:CYS318
|
4.5
|
0.0
|
1.0
|
CA
|
A:VAL328
|
4.6
|
0.0
|
1.0
|
CG1
|
A:VAL328
|
4.6
|
0.0
|
1.0
|
C
|
A:CYS326
|
4.6
|
0.0
|
1.0
|
O
|
A:CYS329
|
4.6
|
0.0
|
1.0
|
N
|
A:VAL328
|
4.6
|
0.0
|
1.0
|
H
|
A:CYS326
|
4.7
|
0.0
|
1.0
|
C
|
A:CYS329
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS315
|
4.7
|
0.0
|
1.0
|
N
|
A:CYS318
|
4.7
|
0.0
|
1.0
|
HG13
|
A:VAL328
|
4.8
|
0.0
|
1.0
|
C
|
A:CYS318
|
4.8
|
0.0
|
1.0
|
HA
|
A:CYS315
|
4.8
|
0.0
|
1.0
|
HA
|
A:VAL322
|
4.8
|
0.0
|
1.0
|
O
|
A:CYS318
|
4.9
|
0.0
|
1.0
|
HA
|
A:CYS329
|
4.9
|
0.0
|
1.0
|
N
|
A:CYS326
|
4.9
|
0.0
|
1.0
|
HG23
|
A:VAL328
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 3 in 2lgk
Go back to
Zinc Binding Sites List in 2lgk
Zinc binding site 2 out
of 3 in the uc(Nmr) Structure of UHRF1 Phd Domains in A Complex with Histone H3 Peptide
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of uc(Nmr) Structure of UHRF1 Phd Domains in A Complex with Histone H3 Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn381
b:0.0
occ:1.00
|
NE2
|
A:HIS354
|
2.0
|
0.0
|
1.0
|
SG
|
A:CYS334
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS331
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS357
|
2.3
|
0.0
|
1.0
|
CD2
|
A:HIS354
|
2.3
|
0.0
|
1.0
|
HD2
|
A:HIS354
|
2.5
|
0.0
|
1.0
|
H
|
A:CYS334
|
2.7
|
0.0
|
1.0
|
CE1
|
A:HIS354
|
3.0
|
0.0
|
1.0
|
HB3
|
A:CYS334
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS331
|
3.3
|
0.0
|
1.0
|
H
|
A:GLY335
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS334
|
3.4
|
0.0
|
1.0
|
CG
|
A:HIS354
|
3.4
|
0.0
|
1.0
|
HB3
|
A:CYS331
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS357
|
3.4
|
0.0
|
1.0
|
HB3
|
A:CYS357
|
3.5
|
0.0
|
1.0
|
HB2
|
A:CYS331
|
3.5
|
0.0
|
1.0
|
HB2
|
A:LEU333
|
3.5
|
0.0
|
1.0
|
N
|
A:CYS334
|
3.5
|
0.0
|
1.0
|
HE1
|
A:HIS354
|
3.6
|
0.0
|
1.0
|
HA
|
A:HIS354
|
3.6
|
0.0
|
1.0
|
HB2
|
A:CYS357
|
3.7
|
0.0
|
1.0
|
ND1
|
A:HIS354
|
3.7
|
0.0
|
1.0
|
H
|
A:GLY336
|
4.0
|
0.0
|
1.0
|
CA
|
A:CYS334
|
4.0
|
0.0
|
1.0
|
OH
|
A:TYR356
|
4.1
|
0.0
|
1.0
|
H
|
A:LEU333
|
4.2
|
0.0
|
1.0
|
N
|
A:GLY335
|
4.2
|
0.0
|
1.0
|
HE1
|
A:TYR356
|
4.2
|
0.0
|
1.0
|
HB2
|
A:CYS334
|
4.3
|
0.0
|
1.0
|
CZ
|
A:TYR356
|
4.5
|
0.0
|
1.0
|
CA
|
A:HIS354
|
4.5
|
0.0
|
1.0
|
CE1
|
A:TYR356
|
4.5
|
0.0
|
1.0
|
HD1
|
A:HIS354
|
4.6
|
0.0
|
1.0
|
CB
|
A:LEU333
|
4.6
|
0.0
|
1.0
|
CB
|
A:HIS354
|
4.6
|
0.0
|
1.0
|
C
|
A:CYS334
|
4.6
|
0.0
|
1.0
|
C
|
A:LEU333
|
4.6
|
0.0
|
1.0
|
CA
|
A:CYS331
|
4.7
|
0.0
|
1.0
|
HH
|
A:TYR356
|
4.7
|
0.0
|
1.0
|
N
|
A:LEU333
|
4.8
|
0.0
|
1.0
|
CA
|
A:CYS357
|
4.8
|
0.0
|
1.0
|
HE21
|
A:GLN338
|
4.8
|
0.0
|
1.0
|
N
|
A:GLY336
|
4.9
|
0.0
|
1.0
|
CA
|
A:LEU333
|
4.9
|
0.0
|
1.0
|
HA
|
A:CYS334
|
4.9
|
0.0
|
1.0
|
HA
|
A:CYS357
|
5.0
|
0.0
|
1.0
|
H
|
A:CYS357
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 3 out
of 3 in 2lgk
Go back to
Zinc Binding Sites List in 2lgk
Zinc binding site 3 out
of 3 in the uc(Nmr) Structure of UHRF1 Phd Domains in A Complex with Histone H3 Peptide
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of uc(Nmr) Structure of UHRF1 Phd Domains in A Complex with Histone H3 Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn382
b:0.0
occ:1.00
|
SG
|
A:CYS376
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS349
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS373
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS346
|
2.3
|
0.0
|
1.0
|
H
|
A:CYS373
|
2.9
|
0.0
|
1.0
|
HB2
|
A:GLU348
|
3.2
|
0.0
|
1.0
|
H
|
A:CYS349
|
3.3
|
0.0
|
1.0
|
HB2
|
A:CYS376
|
3.3
|
0.0
|
1.0
|
HB2
|
A:CYS349
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS373
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS376
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS349
|
3.5
|
0.0
|
1.0
|
CB
|
A:CYS373
|
3.5
|
0.0
|
1.0
|
CB
|
A:CYS346
|
3.5
|
0.0
|
1.0
|
H
|
A:CYS376
|
3.6
|
0.0
|
1.0
|
HB3
|
A:CYS346
|
3.6
|
0.0
|
1.0
|
HB2
|
A:CYS346
|
3.7
|
0.0
|
1.0
|
N
|
A:CYS373
|
3.7
|
0.0
|
1.0
|
N
|
A:CYS349
|
3.8
|
0.0
|
1.0
|
N
|
A:CYS376
|
4.1
|
0.0
|
1.0
|
CA
|
A:CYS373
|
4.1
|
0.0
|
1.0
|
HB3
|
A:GLU375
|
4.1
|
0.0
|
1.0
|
CB
|
A:GLU348
|
4.2
|
0.0
|
1.0
|
CA
|
A:CYS349
|
4.3
|
0.0
|
1.0
|
HB3
|
A:CYS376
|
4.3
|
0.0
|
1.0
|
HB3
|
A:TYR372
|
4.3
|
0.0
|
1.0
|
CA
|
A:CYS376
|
4.3
|
0.0
|
1.0
|
HB3
|
A:CYS349
|
4.3
|
0.0
|
1.0
|
HZ
|
A:PHE353
|
4.3
|
0.0
|
1.0
|
HB2
|
A:CYS373
|
4.3
|
0.0
|
1.0
|
O
|
A:CYS373
|
4.4
|
0.0
|
1.0
|
HA
|
A:CYS376
|
4.4
|
0.0
|
1.0
|
HB3
|
A:GLU348
|
4.5
|
0.0
|
1.0
|
HA
|
A:TYR372
|
4.5
|
0.0
|
1.0
|
H
|
A:GLU348
|
4.5
|
0.0
|
1.0
|
HE1
|
A:PHE353
|
4.5
|
0.0
|
1.0
|
C
|
A:GLU348
|
4.6
|
0.0
|
1.0
|
HD1
|
A:TYR372
|
4.6
|
0.0
|
1.0
|
OE1
|
A:GLU348
|
4.6
|
0.0
|
1.0
|
C
|
A:CYS373
|
4.7
|
0.0
|
1.0
|
C
|
A:TYR372
|
4.8
|
0.0
|
1.0
|
HA
|
A:CYS349
|
4.8
|
0.0
|
1.0
|
CA
|
A:GLU348
|
4.8
|
0.0
|
1.0
|
CA
|
A:CYS346
|
4.8
|
0.0
|
1.0
|
N
|
A:GLU348
|
4.9
|
0.0
|
1.0
|
CZ
|
A:PHE353
|
5.0
|
0.0
|
1.0
|
|
Reference:
C.Wang,
J.Shen,
Z.Yang,
P.Chen,
B.Zhao,
W.Hu,
W.Lan,
X.Tong,
H.Wu,
G.Li,
C.Cao.
Structural Basis For Site-Specific Reading of Unmodified R2 of Histone H3 Tail By UHRF1 Phd Finger. Cell Res. V. 21 1379 2011.
ISSN: ISSN 1001-0602
PubMed: 21808299
DOI: 10.1038/CR.2011.123
Page generated: Thu Oct 17 01:50:35 2024
|