Zinc in PDB 2ln0: Structure of Moz
Enzymatic activity of Structure of Moz
All present enzymatic activity of Structure of Moz:
2.3.1.48;
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Moz
(pdb code 2ln0). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Structure of Moz, PDB code: 2ln0:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 2ln0
Go back to
Zinc Binding Sites List in 2ln0
Zinc binding site 1 out
of 4 in the Structure of Moz
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structure of Moz within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn401
b:0.0
occ:1.00
|
ND1
|
A:HIS238
|
2.1
|
0.0
|
1.0
|
SG
|
A:CYS209
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS212
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS241
|
2.3
|
0.0
|
1.0
|
CE1
|
A:HIS238
|
2.8
|
0.0
|
1.0
|
HE1
|
A:HIS238
|
2.9
|
0.0
|
1.0
|
CB
|
A:CYS209
|
3.1
|
0.0
|
1.0
|
HB3
|
A:CYS209
|
3.1
|
0.0
|
1.0
|
HB2
|
A:CYS209
|
3.1
|
0.0
|
1.0
|
OD1
|
A:ASN219
|
3.2
|
0.0
|
1.0
|
H
|
A:CYS212
|
3.2
|
0.0
|
1.0
|
H
|
A:HIS238
|
3.3
|
0.0
|
1.0
|
HB2
|
A:HIS238
|
3.3
|
0.0
|
1.0
|
HB2
|
A:CYS241
|
3.3
|
0.0
|
1.0
|
CG
|
A:HIS238
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS212
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS241
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS212
|
3.4
|
0.0
|
1.0
|
HB2
|
A:PHE211
|
3.6
|
0.0
|
1.0
|
HG3
|
A:ARG220
|
3.6
|
0.0
|
1.0
|
HB3
|
A:CYS241
|
3.6
|
0.0
|
1.0
|
CB
|
A:HIS238
|
3.8
|
0.0
|
1.0
|
N
|
A:CYS212
|
3.9
|
0.0
|
1.0
|
HA
|
A:ASN219
|
3.9
|
0.0
|
1.0
|
H
|
A:ARG220
|
3.9
|
0.0
|
1.0
|
NE2
|
A:HIS238
|
4.1
|
0.0
|
1.0
|
H
|
A:GLY214
|
4.1
|
0.0
|
1.0
|
N
|
A:HIS238
|
4.2
|
0.0
|
1.0
|
CA
|
A:CYS212
|
4.2
|
0.0
|
1.0
|
CG
|
A:ASN219
|
4.2
|
0.0
|
1.0
|
HE
|
A:ARG220
|
4.2
|
0.0
|
1.0
|
HB2
|
A:CYS212
|
4.3
|
0.0
|
1.0
|
CD2
|
A:HIS238
|
4.3
|
0.0
|
1.0
|
H
|
A:PHE211
|
4.4
|
0.0
|
1.0
|
HD23
|
A:LEU227
|
4.4
|
0.0
|
1.0
|
HD2
|
A:PHE211
|
4.5
|
0.0
|
1.0
|
N
|
A:ARG220
|
4.5
|
0.0
|
1.0
|
HA2
|
A:GLY237
|
4.6
|
0.0
|
1.0
|
CA
|
A:CYS209
|
4.6
|
0.0
|
1.0
|
CB
|
A:PHE211
|
4.6
|
0.0
|
1.0
|
CA
|
A:HIS238
|
4.6
|
0.0
|
1.0
|
CG
|
A:ARG220
|
4.7
|
0.0
|
1.0
|
HB3
|
A:HIS238
|
4.7
|
0.0
|
1.0
|
H
|
A:CYS241
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS241
|
4.8
|
0.0
|
1.0
|
O
|
A:GLY214
|
4.8
|
0.0
|
1.0
|
CA
|
A:ASN219
|
4.8
|
0.0
|
1.0
|
HD22
|
A:ASN219
|
4.8
|
0.0
|
1.0
|
C
|
A:PHE211
|
4.8
|
0.0
|
1.0
|
C
|
A:CYS212
|
4.9
|
0.0
|
1.0
|
HA
|
A:CYS209
|
4.9
|
0.0
|
1.0
|
H
|
A:LEU213
|
4.9
|
0.0
|
1.0
|
HE2
|
A:HIS238
|
4.9
|
0.0
|
1.0
|
HG2
|
A:ARG220
|
4.9
|
0.0
|
1.0
|
HA3
|
A:GLY214
|
5.0
|
0.0
|
1.0
|
ND2
|
A:ASN219
|
5.0
|
0.0
|
1.0
|
N
|
A:GLY214
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 4 in 2ln0
Go back to
Zinc Binding Sites List in 2ln0
Zinc binding site 2 out
of 4 in the Structure of Moz
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structure of Moz within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn501
b:0.0
occ:1.00
|
SG
|
A:CYS262
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS233
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS259
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS230
|
2.3
|
0.0
|
1.0
|
HB2
|
A:CYS262
|
2.9
|
0.0
|
1.0
|
H
|
A:CYS233
|
3.0
|
0.0
|
1.0
|
H
|
A:CYS259
|
3.1
|
0.0
|
1.0
|
HB2
|
A:CYS233
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS262
|
3.2
|
0.0
|
1.0
|
HB3
|
A:ASP232
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS259
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS233
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS259
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS230
|
3.5
|
0.0
|
1.0
|
HB3
|
A:CYS230
|
3.7
|
0.0
|
1.0
|
HB2
|
A:CYS230
|
3.7
|
0.0
|
1.0
|
N
|
A:CYS233
|
3.7
|
0.0
|
1.0
|
N
|
A:CYS259
|
3.9
|
0.0
|
1.0
|
HB3
|
A:CYS262
|
3.9
|
0.0
|
1.0
|
H
|
A:ASP232
|
4.1
|
0.0
|
1.0
|
HB2
|
A:ASP232
|
4.1
|
0.0
|
1.0
|
CB
|
A:ASP232
|
4.1
|
0.0
|
1.0
|
CA
|
A:CYS233
|
4.2
|
0.0
|
1.0
|
HB2
|
A:GLU261
|
4.2
|
0.0
|
1.0
|
CA
|
A:CYS259
|
4.2
|
0.0
|
1.0
|
H
|
A:CYS262
|
4.2
|
0.0
|
1.0
|
HB3
|
A:CYS233
|
4.2
|
0.0
|
1.0
|
N
|
A:CYS262
|
4.3
|
0.0
|
1.0
|
HB2
|
A:CYS259
|
4.3
|
0.0
|
1.0
|
CA
|
A:CYS262
|
4.4
|
0.0
|
1.0
|
HA
|
A:GLN258
|
4.5
|
0.0
|
1.0
|
C
|
A:ASP232
|
4.6
|
0.0
|
1.0
|
H
|
A:GLU261
|
4.7
|
0.0
|
1.0
|
HE21
|
A:GLN258
|
4.8
|
0.0
|
1.0
|
CA
|
A:ASP232
|
4.8
|
0.0
|
1.0
|
HA
|
A:CYS233
|
4.8
|
0.0
|
1.0
|
HA
|
A:CYS262
|
4.8
|
0.0
|
1.0
|
H
|
A:GLY234
|
4.8
|
0.0
|
1.0
|
N
|
A:ASP232
|
4.8
|
0.0
|
1.0
|
HB3
|
A:GLN258
|
4.8
|
0.0
|
1.0
|
C
|
A:GLU261
|
4.8
|
0.0
|
1.0
|
C
|
A:CYS259
|
4.8
|
0.0
|
1.0
|
CA
|
A:CYS230
|
4.9
|
0.0
|
1.0
|
C
|
A:GLN258
|
5.0
|
0.0
|
1.0
|
O
|
A:CYS259
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 3 out
of 4 in 2ln0
Go back to
Zinc Binding Sites List in 2ln0
Zinc binding site 3 out
of 4 in the Structure of Moz
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structure of Moz within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn601
b:0.0
occ:1.00
|
SG
|
A:CYS281
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS284
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS310
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS307
|
2.3
|
0.0
|
1.0
|
HB2
|
A:CYS310
|
3.1
|
0.0
|
1.0
|
H
|
A:CYS284
|
3.1
|
0.0
|
1.0
|
HB3
|
A:CYS284
|
3.2
|
0.0
|
1.0
|
H
|
A:CYS307
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS281
|
3.3
|
0.0
|
1.0
|
HB2
|
A:CYS281
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS310
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS284
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS281
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS307
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS307
|
3.5
|
0.0
|
1.0
|
HB2
|
A:SER283
|
3.5
|
0.0
|
1.0
|
HG22
|
A:ILE306
|
3.6
|
0.0
|
1.0
|
H
|
A:CYS310
|
3.6
|
0.0
|
1.0
|
N
|
A:CYS284
|
3.7
|
0.0
|
1.0
|
HB2
|
A:ARG286
|
3.8
|
0.0
|
1.0
|
HB
|
A:ILE309
|
3.9
|
0.0
|
1.0
|
N
|
A:CYS307
|
3.9
|
0.0
|
1.0
|
H
|
A:ARG286
|
4.0
|
0.0
|
1.0
|
CA
|
A:CYS284
|
4.1
|
0.0
|
1.0
|
N
|
A:CYS310
|
4.1
|
0.0
|
1.0
|
HB3
|
A:CYS310
|
4.1
|
0.0
|
1.0
|
HB3
|
A:SER283
|
4.2
|
0.0
|
1.0
|
H
|
A:SER283
|
4.2
|
0.0
|
1.0
|
CA
|
A:CYS307
|
4.2
|
0.0
|
1.0
|
HB2
|
A:CYS284
|
4.2
|
0.0
|
1.0
|
CB
|
A:SER283
|
4.3
|
0.0
|
1.0
|
CA
|
A:CYS310
|
4.3
|
0.0
|
1.0
|
HB2
|
A:CYS307
|
4.3
|
0.0
|
1.0
|
H
|
A:ASP285
|
4.4
|
0.0
|
1.0
|
C
|
A:SER283
|
4.6
|
0.0
|
1.0
|
CG2
|
A:ILE306
|
4.6
|
0.0
|
1.0
|
O
|
A:CYS307
|
4.6
|
0.0
|
1.0
|
HA
|
A:ILE306
|
4.7
|
0.0
|
1.0
|
HE1
|
A:PHE288
|
4.7
|
0.0
|
1.0
|
C
|
A:CYS307
|
4.7
|
0.0
|
1.0
|
HA
|
A:CYS310
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS281
|
4.7
|
0.0
|
1.0
|
C
|
A:CYS284
|
4.8
|
0.0
|
1.0
|
CB
|
A:ARG286
|
4.8
|
0.0
|
1.0
|
HG21
|
A:ILE306
|
4.8
|
0.0
|
1.0
|
HG2
|
A:ARG286
|
4.8
|
0.0
|
1.0
|
CA
|
A:SER283
|
4.8
|
0.0
|
1.0
|
H
|
A:ILE309
|
4.8
|
0.0
|
1.0
|
N
|
A:ASP285
|
4.9
|
0.0
|
1.0
|
HG3
|
A:ARG286
|
4.9
|
0.0
|
1.0
|
N
|
A:SER283
|
4.9
|
0.0
|
1.0
|
N
|
A:ARG286
|
5.0
|
0.0
|
1.0
|
CB
|
A:ILE309
|
5.0
|
0.0
|
1.0
|
C
|
A:ILE309
|
5.0
|
0.0
|
1.0
|
HA
|
A:CYS284
|
5.0
|
0.0
|
1.0
|
HA
|
A:CYS281
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 4 out
of 4 in 2ln0
Go back to
Zinc Binding Sites List in 2ln0
Zinc binding site 4 out
of 4 in the Structure of Moz
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Structure of Moz within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn701
b:0.0
occ:1.00
|
ND1
|
A:HIS289
|
2.1
|
0.0
|
1.0
|
SG
|
A:CYS265
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS268
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS292
|
2.3
|
0.0
|
1.0
|
H
|
A:CYS268
|
2.8
|
0.0
|
1.0
|
CE1
|
A:HIS289
|
2.8
|
0.0
|
1.0
|
HE1
|
A:HIS289
|
2.8
|
0.0
|
1.0
|
HB3
|
A:CYS268
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS265
|
3.2
|
0.0
|
1.0
|
HB2
|
A:CYS265
|
3.2
|
0.0
|
1.0
|
HB3
|
A:CYS265
|
3.3
|
0.0
|
1.0
|
HB2
|
A:HIS289
|
3.3
|
0.0
|
1.0
|
CG
|
A:HIS289
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS268
|
3.3
|
0.0
|
1.0
|
HB2
|
A:CYS292
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS292
|
3.4
|
0.0
|
1.0
|
H
|
A:HIS289
|
3.5
|
0.0
|
1.0
|
HB3
|
A:SER267
|
3.5
|
0.0
|
1.0
|
H
|
A:ARG269
|
3.6
|
0.0
|
1.0
|
HB3
|
A:CYS292
|
3.6
|
0.0
|
1.0
|
N
|
A:CYS268
|
3.6
|
0.0
|
1.0
|
CB
|
A:HIS289
|
3.9
|
0.0
|
1.0
|
CA
|
A:CYS268
|
4.0
|
0.0
|
1.0
|
NE2
|
A:HIS289
|
4.1
|
0.0
|
1.0
|
HB2
|
A:CYS268
|
4.2
|
0.0
|
1.0
|
N
|
A:ARG269
|
4.2
|
0.0
|
1.0
|
CD2
|
A:HIS289
|
4.3
|
0.0
|
1.0
|
N
|
A:HIS289
|
4.3
|
0.0
|
1.0
|
H
|
A:SER267
|
4.5
|
0.0
|
1.0
|
H
|
A:ASP270
|
4.5
|
0.0
|
1.0
|
C
|
A:CYS268
|
4.6
|
0.0
|
1.0
|
CB
|
A:SER267
|
4.6
|
0.0
|
1.0
|
HB3
|
A:HIS289
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS265
|
4.7
|
0.0
|
1.0
|
HA
|
A:PHE288
|
4.7
|
0.0
|
1.0
|
CA
|
A:HIS289
|
4.8
|
0.0
|
1.0
|
C
|
A:SER267
|
4.8
|
0.0
|
1.0
|
CA
|
A:CYS292
|
4.8
|
0.0
|
1.0
|
HB2
|
A:ASP270
|
4.8
|
0.0
|
1.0
|
HE2
|
A:HIS289
|
4.9
|
0.0
|
1.0
|
HA
|
A:CYS268
|
5.0
|
0.0
|
1.0
|
N
|
A:SER267
|
5.0
|
0.0
|
1.0
|
HA
|
A:CYS292
|
5.0
|
0.0
|
1.0
|
HA
|
A:CYS265
|
5.0
|
0.0
|
1.0
|
|
Reference:
Y.Qiu,
L.Liu,
C.Zhao,
C.Han,
F.Li,
J.Zhang,
Y.Wang,
G.Li,
Y.Mei,
M.Wu,
J.Wu,
Y.Shi.
Combinatorial Readout of Unmodified H3R2 and Acetylated H3K14 By the Tandem Phd Finger of Moz Reveals A Regulatory Mechanism For HOXA9 Transcription. Genes Dev. V. 26 1376 2012.
ISSN: ISSN 0890-9369
PubMed: 22713874
DOI: 10.1101/GAD.188359.112
Page generated: Thu Oct 17 01:52:57 2024
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