Zinc in PDB 2m1r: Phd Domain of ING4 N214D Mutant
Zinc Binding Sites:
The binding sites of Zinc atom in the Phd Domain of ING4 N214D Mutant
(pdb code 2m1r). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Phd Domain of ING4 N214D Mutant, PDB code: 2m1r:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 2m1r
Go back to
Zinc Binding Sites List in 2m1r
Zinc binding site 1 out
of 2 in the Phd Domain of ING4 N214D Mutant
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Phd Domain of ING4 N214D Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:0.0
occ:1.00
|
HB2
|
A:HIS223
|
2.0
|
0.0
|
1.0
|
HB2
|
A:CYS201
|
2.2
|
0.0
|
1.0
|
OH
|
A:TYR206
|
2.2
|
0.0
|
1.0
|
HB2
|
A:CYS199
|
2.2
|
0.0
|
1.0
|
HH
|
A:TYR206
|
2.4
|
0.0
|
1.0
|
SG
|
A:CYS201
|
2.5
|
0.0
|
1.0
|
SG
|
A:CYS226
|
2.5
|
0.0
|
1.0
|
HB3
|
A:HIS223
|
2.7
|
0.0
|
1.0
|
CB
|
A:CYS201
|
2.7
|
0.0
|
1.0
|
CB
|
A:HIS223
|
2.8
|
0.0
|
1.0
|
H
|
A:CYS201
|
2.9
|
0.0
|
1.0
|
CB
|
A:CYS199
|
3.0
|
0.0
|
1.0
|
HB3
|
A:CYS199
|
3.1
|
0.0
|
1.0
|
H
|
A:HIS223
|
3.2
|
0.0
|
1.0
|
CG
|
A:HIS223
|
3.4
|
0.0
|
1.0
|
HG
|
A:CYS226
|
3.4
|
0.0
|
1.0
|
N
|
A:CYS201
|
3.5
|
0.0
|
1.0
|
CZ
|
A:TYR206
|
3.5
|
0.0
|
1.0
|
HB3
|
A:CYS201
|
3.5
|
0.0
|
1.0
|
ND1
|
A:HIS223
|
3.6
|
0.0
|
1.0
|
SG
|
A:CYS199
|
3.6
|
0.0
|
1.0
|
CA
|
A:CYS201
|
3.8
|
0.0
|
1.0
|
HH2
|
A:TRP221
|
3.8
|
0.0
|
1.0
|
H
|
A:LEU200
|
3.8
|
0.0
|
1.0
|
N
|
A:HIS223
|
3.9
|
0.0
|
1.0
|
CA
|
A:HIS223
|
4.0
|
0.0
|
1.0
|
HZ2
|
A:TRP221
|
4.0
|
0.0
|
1.0
|
CB
|
A:CYS226
|
4.1
|
0.0
|
1.0
|
HE2
|
A:TYR206
|
4.1
|
0.0
|
1.0
|
HB2
|
A:CYS226
|
4.1
|
0.0
|
1.0
|
CH2
|
A:TRP221
|
4.3
|
0.0
|
1.0
|
CE2
|
A:TYR206
|
4.3
|
0.0
|
1.0
|
N
|
A:LEU200
|
4.3
|
0.0
|
1.0
|
CZ2
|
A:TRP221
|
4.3
|
0.0
|
1.0
|
CA
|
A:CYS199
|
4.4
|
0.0
|
1.0
|
HE1
|
A:TYR206
|
4.4
|
0.0
|
1.0
|
CE1
|
A:TYR206
|
4.5
|
0.0
|
1.0
|
HA
|
A:CYS201
|
4.5
|
0.0
|
1.0
|
HA
|
A:HIS223
|
4.5
|
0.0
|
1.0
|
CD2
|
A:HIS223
|
4.5
|
0.0
|
1.0
|
C
|
A:LEU200
|
4.5
|
0.0
|
1.0
|
H
|
A:HIS202
|
4.5
|
0.0
|
1.0
|
H
|
A:CYS226
|
4.6
|
0.0
|
1.0
|
HA
|
A:CYS199
|
4.7
|
0.0
|
1.0
|
C
|
A:CYS199
|
4.7
|
0.0
|
1.0
|
O
|
A:GLN203
|
4.7
|
0.0
|
1.0
|
CE1
|
A:HIS223
|
4.7
|
0.0
|
1.0
|
HB2
|
A:LEU200
|
4.7
|
0.0
|
1.0
|
HA
|
A:PHE222
|
4.7
|
0.0
|
1.0
|
HB3
|
A:CYS226
|
4.8
|
0.0
|
1.0
|
C
|
A:CYS201
|
4.8
|
0.0
|
1.0
|
N
|
A:CYS226
|
4.8
|
0.0
|
1.0
|
HA
|
A:CYS226
|
4.8
|
0.0
|
1.0
|
CA
|
A:CYS226
|
4.9
|
0.0
|
1.0
|
HG2
|
A:GLN203
|
4.9
|
0.0
|
1.0
|
CA
|
A:LEU200
|
5.0
|
0.0
|
1.0
|
H
|
A:GLN203
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 2m1r
Go back to
Zinc Binding Sites List in 2m1r
Zinc binding site 2 out
of 2 in the Phd Domain of ING4 N214D Mutant
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Phd Domain of ING4 N214D Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn302
b:0.0
occ:1.00
|
HB3
|
A:CYS212
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS217
|
2.3
|
0.0
|
1.0
|
HB2
|
A:CYS212
|
2.4
|
0.0
|
1.0
|
SG
|
A:CYS239
|
2.4
|
0.0
|
1.0
|
HE1
|
A:PHE222
|
2.4
|
0.0
|
1.0
|
HB3
|
A:CYS239
|
2.7
|
0.0
|
1.0
|
CB
|
A:CYS212
|
2.7
|
0.0
|
1.0
|
HG
|
A:CYS217
|
2.7
|
0.0
|
1.0
|
HZ
|
A:PHE222
|
2.9
|
0.0
|
1.0
|
CE1
|
A:PHE222
|
3.0
|
0.0
|
1.0
|
CB
|
A:CYS239
|
3.1
|
0.0
|
1.0
|
CZ
|
A:PHE222
|
3.2
|
0.0
|
1.0
|
H
|
A:CYS239
|
3.3
|
0.0
|
1.0
|
SG
|
A:CYS212
|
3.4
|
0.0
|
1.0
|
SG
|
A:CYS242
|
3.4
|
0.0
|
1.0
|
HB2
|
A:CYS217
|
3.5
|
0.0
|
1.0
|
CB
|
A:CYS217
|
3.6
|
0.0
|
1.0
|
HG
|
A:CYS239
|
3.7
|
0.0
|
1.0
|
HB2
|
A:CYS239
|
3.7
|
0.0
|
1.0
|
HB
|
A:ILE219
|
3.9
|
0.0
|
1.0
|
HB2
|
A:CYS242
|
4.0
|
0.0
|
1.0
|
H
|
A:CYS212
|
4.0
|
0.0
|
1.0
|
CD1
|
A:PHE222
|
4.1
|
0.0
|
1.0
|
N
|
A:CYS239
|
4.1
|
0.0
|
1.0
|
CA
|
A:CYS212
|
4.1
|
0.0
|
1.0
|
CA
|
A:CYS239
|
4.2
|
0.0
|
1.0
|
H
|
A:GLU220
|
4.3
|
0.0
|
1.0
|
HB3
|
A:CYS217
|
4.3
|
0.0
|
1.0
|
CB
|
A:CYS242
|
4.4
|
0.0
|
1.0
|
CE2
|
A:PHE222
|
4.4
|
0.0
|
1.0
|
HD1
|
A:PHE222
|
4.4
|
0.0
|
1.0
|
HA
|
A:CYS217
|
4.5
|
0.0
|
1.0
|
H
|
A:CYS242
|
4.5
|
0.0
|
1.0
|
N
|
A:CYS212
|
4.5
|
0.0
|
1.0
|
HB3
|
A:ASP214
|
4.5
|
0.0
|
1.0
|
HG
|
A:CYS242
|
4.7
|
0.0
|
1.0
|
HZ3
|
A:TRP237
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS217
|
4.7
|
0.0
|
1.0
|
HA
|
A:CYS212
|
4.7
|
0.0
|
1.0
|
H
|
A:ILE219
|
4.7
|
0.0
|
1.0
|
HB2
|
A:ARG241
|
4.9
|
0.0
|
1.0
|
CB
|
A:ILE219
|
4.9
|
0.0
|
1.0
|
HB3
|
A:CYS242
|
5.0
|
0.0
|
1.0
|
HE2
|
A:PHE222
|
5.0
|
0.0
|
1.0
|
HA
|
A:CYS239
|
5.0
|
0.0
|
1.0
|
|
Reference:
A.Moreno,
A.Palacios,
J.L.Orgaz,
B.Jimenez,
F.J.Blanco,
I.Palmero.
Functional Impact of Cancer-Associated Mutations in the Tumor Suppressor Protein ING4. Carcinogenesis V. 31 1932 2010.
PubMed: 20705953
DOI: 10.1093/CARCIN/BGQ171
Page generated: Thu Oct 17 01:58:38 2024
|