Zinc in PDB 2fuu: uc(Nmr) Solution Structure of the Phd Domain From the Human Bptf in Complex with H3(1-15)K4ME3 Peptide
Zinc Binding Sites:
The binding sites of Zinc atom in the uc(Nmr) Solution Structure of the Phd Domain From the Human Bptf in Complex with H3(1-15)K4ME3 Peptide
(pdb code 2fuu). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
uc(Nmr) Solution Structure of the Phd Domain From the Human Bptf in Complex with H3(1-15)K4ME3 Peptide, PDB code: 2fuu:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 2fuu
Go back to
Zinc Binding Sites List in 2fuu
Zinc binding site 1 out
of 2 in the uc(Nmr) Solution Structure of the Phd Domain From the Human Bptf in Complex with H3(1-15)K4ME3 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) Solution Structure of the Phd Domain From the Human Bptf in Complex with H3(1-15)K4ME3 Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn201
b:0.0
occ:1.00
|
SG
|
A:CYS56
|
1.2
|
16.7
|
1.0
|
SG
|
A:CYS53
|
1.4
|
16.7
|
1.0
|
SG
|
A:CYS29
|
1.5
|
16.7
|
1.0
|
SG
|
A:CYS26
|
1.6
|
16.7
|
1.0
|
H
|
A:CYS29
|
1.8
|
0.0
|
1.0
|
H
|
A:CYS53
|
2.0
|
0.0
|
1.0
|
CB
|
A:CYS56
|
2.4
|
16.7
|
1.0
|
HB2
|
A:CYS56
|
2.4
|
0.0
|
1.0
|
HG13
|
A:VAL52
|
2.5
|
0.0
|
1.0
|
H
|
A:ARG28
|
2.5
|
0.0
|
1.0
|
N
|
A:CYS29
|
2.6
|
16.7
|
1.0
|
CB
|
A:CYS26
|
2.7
|
16.7
|
1.0
|
CB
|
A:CYS53
|
2.8
|
16.7
|
1.0
|
HA
|
A:CYS26
|
2.8
|
0.0
|
1.0
|
N
|
A:CYS53
|
2.9
|
16.7
|
1.0
|
HG11
|
A:VAL52
|
2.9
|
0.0
|
1.0
|
HB3
|
A:CYS56
|
2.9
|
0.0
|
1.0
|
CA
|
A:CYS26
|
3.0
|
16.7
|
1.0
|
CB
|
A:CYS29
|
3.1
|
16.7
|
1.0
|
HB3
|
A:CYS26
|
3.1
|
0.0
|
1.0
|
CG1
|
A:VAL52
|
3.1
|
50.0
|
1.0
|
HB3
|
A:CYS53
|
3.2
|
0.0
|
1.0
|
HB3
|
A:ARG28
|
3.2
|
0.0
|
1.0
|
C
|
A:CYS26
|
3.3
|
16.7
|
1.0
|
H
|
A:CYS56
|
3.3
|
0.0
|
1.0
|
N
|
A:ARG28
|
3.3
|
16.7
|
1.0
|
CA
|
A:CYS53
|
3.3
|
16.7
|
1.0
|
H
|
A:ASP27
|
3.3
|
0.0
|
1.0
|
CA
|
A:CYS29
|
3.4
|
16.7
|
1.0
|
H
|
A:GLN57
|
3.4
|
0.0
|
1.0
|
N
|
A:ASP27
|
3.4
|
16.7
|
1.0
|
HB2
|
A:CYS26
|
3.6
|
0.0
|
1.0
|
C
|
A:ARG28
|
3.6
|
16.7
|
1.0
|
CA
|
A:CYS56
|
3.6
|
16.7
|
1.0
|
H
|
A:GLN30
|
3.6
|
0.0
|
1.0
|
HB2
|
A:CYS53
|
3.6
|
0.0
|
1.0
|
O
|
A:CYS53
|
3.6
|
16.7
|
1.0
|
HB3
|
A:CYS29
|
3.7
|
0.0
|
1.0
|
HG12
|
A:VAL52
|
3.7
|
0.0
|
1.0
|
HB2
|
A:CYS29
|
3.7
|
0.0
|
1.0
|
CA
|
A:ARG28
|
3.8
|
16.7
|
1.0
|
C
|
A:CYS53
|
3.8
|
16.7
|
1.0
|
N
|
A:CYS56
|
3.8
|
16.7
|
1.0
|
CB
|
A:ARG28
|
4.0
|
16.7
|
1.0
|
O
|
A:CYS26
|
4.0
|
16.7
|
1.0
|
N
|
A:GLN57
|
4.0
|
16.7
|
1.0
|
HA
|
A:VAL52
|
4.0
|
0.0
|
1.0
|
C
|
A:VAL52
|
4.0
|
16.7
|
1.0
|
HG2
|
A:ARG28
|
4.1
|
0.0
|
1.0
|
HA
|
A:CYS29
|
4.2
|
0.0
|
1.0
|
C
|
A:CYS56
|
4.2
|
16.7
|
1.0
|
HA
|
A:CYS53
|
4.3
|
0.0
|
1.0
|
C
|
A:ASP27
|
4.3
|
16.7
|
1.0
|
N
|
A:GLN30
|
4.4
|
16.7
|
1.0
|
CA
|
A:VAL52
|
4.4
|
16.7
|
1.0
|
CB
|
A:VAL52
|
4.4
|
50.0
|
1.0
|
N
|
A:CYS26
|
4.4
|
16.7
|
1.0
|
C
|
A:CYS29
|
4.4
|
16.7
|
1.0
|
HA
|
A:CYS56
|
4.4
|
0.0
|
1.0
|
CA
|
A:ASP27
|
4.4
|
16.7
|
1.0
|
OH
|
A:TYR33
|
4.5
|
50.0
|
1.0
|
CG
|
A:ARG28
|
4.6
|
16.7
|
1.0
|
HB2
|
A:GLN57
|
4.7
|
0.0
|
1.0
|
H
|
A:ASN31
|
4.7
|
0.0
|
1.0
|
O
|
A:ARG28
|
4.7
|
16.7
|
1.0
|
HB3
|
A:ASP27
|
4.7
|
0.0
|
1.0
|
HD2
|
A:ARG28
|
4.8
|
0.0
|
1.0
|
HH
|
A:TYR33
|
4.8
|
0.0
|
1.0
|
HA
|
A:ARG28
|
4.9
|
0.0
|
1.0
|
H
|
A:CYS26
|
4.9
|
0.0
|
1.0
|
HB2
|
A:ARG28
|
4.9
|
0.0
|
1.0
|
HB
|
A:VAL52
|
4.9
|
0.0
|
1.0
|
N
|
A:PRO54
|
4.9
|
16.7
|
1.0
|
H
|
A:GLN55
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 2fuu
Go back to
Zinc Binding Sites List in 2fuu
Zinc binding site 2 out
of 2 in the uc(Nmr) Solution Structure of the Phd Domain From the Human Bptf in Complex with H3(1-15)K4ME3 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) Solution Structure of the Phd Domain From the Human Bptf in Complex with H3(1-15)K4ME3 Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn202
b:0.0
occ:1.00
|
SG
|
A:CYS37
|
1.3
|
16.7
|
1.0
|
SG
|
A:CYS13
|
1.4
|
16.7
|
1.0
|
SG
|
A:CYS11
|
1.6
|
16.7
|
1.0
|
CB
|
A:CYS37
|
2.4
|
16.7
|
1.0
|
HB2
|
A:CYS37
|
2.5
|
0.0
|
1.0
|
CB
|
A:CYS13
|
2.5
|
16.7
|
1.0
|
ND1
|
A:HIS34
|
2.6
|
16.7
|
1.0
|
HB2
|
A:CYS13
|
2.6
|
0.0
|
1.0
|
CE1
|
A:HIS34
|
2.7
|
16.7
|
1.0
|
CB
|
A:CYS11
|
2.7
|
16.7
|
1.0
|
HE1
|
A:HIS34
|
2.9
|
0.0
|
1.0
|
HA
|
A:CYS37
|
2.9
|
0.0
|
1.0
|
HB2
|
A:CYS11
|
2.9
|
0.0
|
1.0
|
HB3
|
A:CYS11
|
3.0
|
0.0
|
1.0
|
HB3
|
A:CYS13
|
3.1
|
0.0
|
1.0
|
H
|
A:HIS34
|
3.1
|
0.0
|
1.0
|
CA
|
A:CYS37
|
3.2
|
16.7
|
1.0
|
H
|
A:CYS13
|
3.2
|
0.0
|
1.0
|
HB3
|
A:CYS37
|
3.2
|
0.0
|
1.0
|
CG
|
A:HIS34
|
3.3
|
16.7
|
1.0
|
NE2
|
A:HIS34
|
3.5
|
16.7
|
1.0
|
CA
|
A:CYS13
|
3.8
|
16.7
|
1.0
|
CD2
|
A:HIS34
|
3.8
|
16.7
|
1.0
|
N
|
A:CYS13
|
3.9
|
16.7
|
1.0
|
HB2
|
A:HIS34
|
3.9
|
0.0
|
1.0
|
HB3
|
A:TYR33
|
4.0
|
0.0
|
1.0
|
CA
|
A:CYS11
|
4.1
|
16.7
|
1.0
|
N
|
A:HIS34
|
4.1
|
16.7
|
1.0
|
HE2
|
A:HIS34
|
4.1
|
0.0
|
1.0
|
CB
|
A:HIS34
|
4.1
|
16.7
|
1.0
|
C
|
A:CYS37
|
4.2
|
16.7
|
1.0
|
N
|
A:CYS37
|
4.2
|
16.7
|
1.0
|
HA
|
A:CYS11
|
4.2
|
0.0
|
1.0
|
OG1
|
A:THR15
|
4.3
|
50.0
|
1.0
|
HZ2
|
A:LYS21
|
4.3
|
0.0
|
1.0
|
H
|
A:CYS37
|
4.4
|
0.0
|
1.0
|
O
|
A:CYS37
|
4.4
|
16.7
|
1.0
|
HB
|
A:THR15
|
4.4
|
0.0
|
1.0
|
C
|
A:CYS13
|
4.4
|
16.7
|
1.0
|
C
|
A:CYS11
|
4.4
|
16.7
|
1.0
|
HG12
|
A:ILE12
|
4.5
|
0.0
|
1.0
|
HA
|
A:CYS13
|
4.6
|
0.0
|
1.0
|
O
|
A:CYS13
|
4.6
|
16.7
|
1.0
|
HD2
|
A:HIS34
|
4.6
|
0.0
|
1.0
|
H
|
A:ILE12
|
4.7
|
0.0
|
1.0
|
CA
|
A:HIS34
|
4.7
|
16.7
|
1.0
|
N
|
A:ILE12
|
4.7
|
16.7
|
1.0
|
HA
|
A:TYR33
|
4.7
|
0.0
|
1.0
|
HE3
|
A:LYS21
|
4.8
|
0.0
|
1.0
|
CB
|
A:TYR33
|
4.9
|
16.7
|
1.0
|
O
|
A:HIS34
|
4.9
|
16.7
|
1.0
|
NZ
|
A:LYS21
|
4.9
|
50.0
|
1.0
|
CB
|
A:THR15
|
4.9
|
50.0
|
1.0
|
O
|
A:CYS11
|
4.9
|
16.7
|
1.0
|
HB2
|
A:TYR33
|
5.0
|
0.0
|
1.0
|
|
Reference:
H.Li,
S.Ilin,
W.Wang,
E.M.Duncan,
J.Wysocka,
C.D.Allis,
D.J.Patel.
Molecular Basis For Site-Specific Read-Out of Histone H3K4ME3 By the Bptf Phd Finger of Nurf. Nature V. 442 91 2006.
ISSN: ISSN 0028-0836
PubMed: 16728978
DOI: 10.1038/NATURE04802
Page generated: Wed Oct 16 23:55:32 2024
|