Zinc in PDB 2jw6: Solution Structure of the DEAF1 Mynd Domain
Zinc Binding Sites:
The binding sites of Zinc atom in the Solution Structure of the DEAF1 Mynd Domain
(pdb code 2jw6). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Solution Structure of the DEAF1 Mynd Domain, PDB code: 2jw6:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 2jw6
Go back to
Zinc Binding Sites List in 2jw6
Zinc binding site 1 out
of 2 in the Solution Structure of the DEAF1 Mynd Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Solution Structure of the DEAF1 Mynd Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn601
b:0.3
occ:1.00
|
SG
|
A:CYS528
|
2.3
|
0.4
|
1.0
|
SG
|
A:CYS507
|
2.3
|
0.5
|
1.0
|
SG
|
A:CYS524
|
2.3
|
0.3
|
1.0
|
SG
|
A:CYS504
|
2.3
|
0.3
|
1.0
|
H
|
A:CYS524
|
2.7
|
0.2
|
1.0
|
H
|
A:SER525
|
2.9
|
0.2
|
1.0
|
HB3
|
A:ASN506
|
3.0
|
0.5
|
1.0
|
HB3
|
A:CYS528
|
3.1
|
0.8
|
1.0
|
HB2
|
A:CYS507
|
3.2
|
1.0
|
1.0
|
H
|
A:CYS507
|
3.3
|
0.5
|
1.0
|
CB
|
A:CYS528
|
3.3
|
0.6
|
1.0
|
CB
|
A:CYS507
|
3.3
|
0.6
|
1.0
|
H
|
A:GLY508
|
3.4
|
0.7
|
1.0
|
CB
|
A:CYS524
|
3.4
|
0.3
|
1.0
|
CB
|
A:CYS504
|
3.5
|
0.2
|
1.0
|
N
|
A:CYS524
|
3.5
|
0.1
|
1.0
|
HB3
|
A:TYR523
|
3.5
|
0.3
|
1.0
|
HB2
|
A:CYS504
|
3.5
|
0.3
|
1.0
|
HB3
|
A:CYS524
|
3.5
|
0.3
|
1.0
|
N
|
A:CYS507
|
3.6
|
0.5
|
1.0
|
HB3
|
A:CYS504
|
3.7
|
0.3
|
1.0
|
HB2
|
A:CYS528
|
3.7
|
0.8
|
1.0
|
N
|
A:SER525
|
3.8
|
0.2
|
1.0
|
CA
|
A:CYS524
|
3.9
|
0.2
|
1.0
|
HD2
|
A:TYR523
|
4.0
|
0.6
|
1.0
|
CA
|
A:CYS507
|
4.0
|
0.6
|
1.0
|
CB
|
A:ASN506
|
4.1
|
0.6
|
1.0
|
HE1
|
A:PHE527
|
4.1
|
0.5
|
1.0
|
HB3
|
A:CYS507
|
4.2
|
0.9
|
1.0
|
HZ
|
A:PHE527
|
4.3
|
0.5
|
1.0
|
N
|
A:GLY508
|
4.3
|
0.7
|
1.0
|
HB3
|
A:SER525
|
4.3
|
0.9
|
1.0
|
HB2
|
A:CYS524
|
4.3
|
0.4
|
1.0
|
C
|
A:CYS524
|
4.4
|
0.2
|
1.0
|
CE1
|
A:PHE527
|
4.4
|
0.4
|
1.0
|
C
|
A:ASN506
|
4.4
|
0.6
|
1.0
|
OD1
|
A:ASN506
|
4.4
|
1.4
|
1.0
|
H
|
A:ASN506
|
4.4
|
0.5
|
1.0
|
CZ
|
A:PHE527
|
4.4
|
0.4
|
1.0
|
H
|
A:CYS528
|
4.5
|
0.3
|
1.0
|
CB
|
A:TYR523
|
4.5
|
0.4
|
1.0
|
C
|
A:TYR523
|
4.5
|
0.2
|
1.0
|
CA
|
A:CYS528
|
4.6
|
0.4
|
1.0
|
HA
|
A:TYR523
|
4.6
|
0.2
|
1.0
|
CG
|
A:ASN506
|
4.6
|
0.7
|
1.0
|
CA
|
A:ASN506
|
4.7
|
0.6
|
1.0
|
C
|
A:CYS507
|
4.7
|
0.7
|
1.0
|
HB2
|
A:SER525
|
4.7
|
1.0
|
1.0
|
HB2
|
A:ASN506
|
4.7
|
0.7
|
1.0
|
CA
|
A:SER525
|
4.8
|
0.2
|
1.0
|
CA
|
A:CYS504
|
4.8
|
0.3
|
1.0
|
CB
|
A:SER525
|
4.8
|
0.3
|
1.0
|
CA
|
A:TYR523
|
4.8
|
0.2
|
1.0
|
HA
|
A:CYS528
|
4.8
|
0.5
|
1.0
|
HA
|
A:CYS524
|
4.9
|
0.2
|
1.0
|
HA
|
A:CYS507
|
4.9
|
0.6
|
1.0
|
N
|
A:ASN506
|
4.9
|
0.5
|
1.0
|
O
|
A:SER525
|
4.9
|
0.2
|
1.0
|
CD2
|
A:TYR523
|
5.0
|
0.6
|
1.0
|
HA
|
A:CYS504
|
5.0
|
0.4
|
1.0
|
|
Zinc binding site 2 out
of 2 in 2jw6
Go back to
Zinc Binding Sites List in 2jw6
Zinc binding site 2 out
of 2 in the Solution Structure of the DEAF1 Mynd Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Solution Structure of the DEAF1 Mynd Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn602
b:0.3
occ:1.00
|
NE2
|
A:HIS536
|
2.0
|
0.4
|
1.0
|
SG
|
A:CYS515
|
2.3
|
0.4
|
1.0
|
SG
|
A:CYS540
|
2.3
|
0.3
|
1.0
|
SG
|
A:CYS518
|
2.3
|
0.3
|
1.0
|
CE1
|
A:HIS536
|
2.9
|
0.5
|
1.0
|
CD2
|
A:HIS536
|
3.0
|
0.4
|
1.0
|
HB3
|
A:CYS515
|
3.2
|
0.3
|
1.0
|
HE1
|
A:HIS536
|
3.2
|
0.6
|
1.0
|
HB2
|
A:CYS540
|
3.2
|
0.3
|
1.0
|
HD2
|
A:HIS536
|
3.2
|
0.6
|
1.0
|
HB3
|
A:CYS518
|
3.2
|
0.4
|
1.0
|
CB
|
A:CYS540
|
3.3
|
0.3
|
1.0
|
CB
|
A:CYS515
|
3.4
|
0.3
|
1.0
|
CB
|
A:CYS518
|
3.4
|
0.3
|
1.0
|
HA
|
A:CYS540
|
3.5
|
0.5
|
1.0
|
HZ3
|
A:TRP533
|
3.7
|
0.4
|
1.0
|
HG23
|
A:VAL521
|
3.8
|
1.1
|
1.0
|
HE3
|
A:TRP533
|
3.8
|
0.4
|
1.0
|
HB2
|
A:CYS515
|
3.8
|
0.4
|
1.0
|
H
|
A:HIS519
|
3.9
|
0.3
|
1.0
|
CA
|
A:CYS540
|
4.0
|
0.4
|
1.0
|
H
|
A:LYS520
|
4.0
|
0.3
|
1.0
|
H
|
A:GLY517
|
4.0
|
0.4
|
1.0
|
N
|
A:CYS518
|
4.0
|
0.3
|
1.0
|
ND1
|
A:HIS536
|
4.0
|
0.5
|
1.0
|
CG
|
A:HIS536
|
4.1
|
0.4
|
1.0
|
H
|
A:CYS518
|
4.1
|
0.3
|
1.0
|
HB2
|
A:LYS520
|
4.2
|
0.3
|
1.0
|
HB2
|
A:CYS518
|
4.2
|
0.4
|
1.0
|
HB3
|
A:CYS540
|
4.2
|
0.4
|
1.0
|
HA3
|
A:GLY517
|
4.2
|
0.4
|
1.0
|
C
|
A:GLY517
|
4.3
|
0.4
|
1.0
|
CA
|
A:CYS518
|
4.3
|
0.3
|
1.0
|
H
|
A:GLY541
|
4.4
|
0.7
|
1.0
|
O
|
A:CYS515
|
4.4
|
0.3
|
1.0
|
CZ3
|
A:TRP533
|
4.5
|
0.5
|
1.0
|
CE3
|
A:TRP533
|
4.5
|
0.4
|
1.0
|
CA
|
A:GLY517
|
4.6
|
0.4
|
1.0
|
N
|
A:HIS519
|
4.7
|
0.2
|
1.0
|
CA
|
A:CYS515
|
4.7
|
0.3
|
1.0
|
CG2
|
A:VAL521
|
4.7
|
0.3
|
1.0
|
N
|
A:GLY517
|
4.7
|
0.3
|
1.0
|
C
|
A:CYS515
|
4.7
|
0.3
|
1.0
|
HG21
|
A:VAL521
|
4.7
|
1.0
|
1.0
|
O
|
A:GLY517
|
4.8
|
0.4
|
1.0
|
N
|
A:CYS540
|
4.9
|
0.4
|
1.0
|
HD1
|
A:HIS536
|
4.9
|
0.7
|
1.0
|
N
|
A:LYS520
|
5.0
|
0.2
|
1.0
|
HG22
|
A:VAL521
|
5.0
|
0.9
|
1.0
|
|
Reference:
R.Spadaccini,
H.Perrin,
M.J.Bottomley,
S.Ansieau,
M.Sattler.
Retraction Notice to "Structure and Functional Analysis of the Mynd Domain" [J. Mol. Biol. (2006) 358, 498-508]. J.Mol.Biol. V. 376 1523 2008.
ISSN: ISSN 0022-2836
PubMed: 18286714
Page generated: Thu Oct 17 01:27:23 2024
|