Zinc in PDB 2kje: uc(Nmr) Structure of Cbp TAZ2 and Adenoviral E1A Complex
Enzymatic activity of uc(Nmr) Structure of Cbp TAZ2 and Adenoviral E1A Complex
All present enzymatic activity of uc(Nmr) Structure of Cbp TAZ2 and Adenoviral E1A Complex:
2.3.1.48;
Zinc Binding Sites:
The binding sites of Zinc atom in the uc(Nmr) Structure of Cbp TAZ2 and Adenoviral E1A Complex
(pdb code 2kje). 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 Cbp TAZ2 and Adenoviral E1A Complex, PDB code: 2kje:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 2kje
Go back to
Zinc Binding Sites List in 2kje
Zinc binding site 1 out
of 3 in the uc(Nmr) Structure of Cbp TAZ2 and Adenoviral E1A Complex
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 Cbp TAZ2 and Adenoviral E1A Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn500
b:0.0
occ:1.00
|
NE2
|
A:HIS1782
|
2.1
|
0.0
|
1.0
|
SG
|
A:CYS1786
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS1796
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS1791
|
2.3
|
0.0
|
1.0
|
HB3
|
A:CYS1791
|
2.8
|
0.0
|
1.0
|
CD2
|
A:HIS1782
|
2.9
|
0.0
|
1.0
|
HD2
|
A:HIS1782
|
2.9
|
0.0
|
1.0
|
CB
|
A:CYS1791
|
2.9
|
0.0
|
1.0
|
HB2
|
A:CYS1796
|
3.0
|
0.0
|
1.0
|
HB2
|
A:CYS1791
|
3.0
|
0.0
|
1.0
|
HB2
|
A:CYS1786
|
3.1
|
0.0
|
1.0
|
CB
|
A:CYS1796
|
3.1
|
0.0
|
1.0
|
CE1
|
A:HIS1782
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS1786
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS1796
|
3.4
|
0.0
|
1.0
|
HE1
|
A:HIS1782
|
3.7
|
0.0
|
1.0
|
HB3
|
A:LEU1793
|
3.7
|
0.0
|
1.0
|
HZ2
|
A:LYS1800
|
3.7
|
0.0
|
1.0
|
HB3
|
A:CYS1786
|
3.8
|
0.0
|
1.0
|
CG
|
A:HIS1782
|
4.1
|
0.0
|
1.0
|
ND1
|
A:HIS1782
|
4.3
|
0.0
|
1.0
|
HA
|
A:ALA1783
|
4.3
|
0.0
|
1.0
|
HZ1
|
A:LYS1800
|
4.4
|
0.0
|
1.0
|
CA
|
A:CYS1791
|
4.4
|
0.0
|
1.0
|
HB2
|
A:LEU1793
|
4.5
|
0.0
|
1.0
|
NZ
|
A:LYS1800
|
4.5
|
0.0
|
1.0
|
HA
|
A:CYS1786
|
4.6
|
0.0
|
1.0
|
CA
|
A:CYS1796
|
4.6
|
0.0
|
1.0
|
CB
|
A:LEU1793
|
4.6
|
0.0
|
1.0
|
CA
|
A:CYS1786
|
4.6
|
0.0
|
1.0
|
H
|
A:LEU1793
|
4.6
|
0.0
|
1.0
|
HA
|
A:CYS1796
|
4.8
|
0.0
|
1.0
|
HG
|
A:LEU1793
|
4.8
|
0.0
|
1.0
|
HE3
|
A:LYS1800
|
4.8
|
0.0
|
1.0
|
HD13
|
A:LEU1793
|
4.8
|
0.0
|
1.0
|
HA
|
A:CYS1791
|
4.8
|
0.0
|
1.0
|
O
|
A:ASN1788
|
4.9
|
0.0
|
1.0
|
H
|
A:CYS1791
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 3 in 2kje
Go back to
Zinc Binding Sites List in 2kje
Zinc binding site 2 out
of 3 in the uc(Nmr) Structure of Cbp TAZ2 and Adenoviral E1A Complex
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 Cbp TAZ2 and Adenoviral E1A Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn501
b:0.0
occ:1.00
|
NE2
|
A:HIS1805
|
2.1
|
0.0
|
1.0
|
SG
|
A:CYS1817
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS1809
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS1820
|
2.3
|
0.0
|
1.0
|
CD2
|
A:HIS1805
|
2.8
|
0.0
|
1.0
|
HD2
|
A:HIS1805
|
2.8
|
0.0
|
1.0
|
HB2
|
A:CYS1809
|
2.9
|
0.0
|
1.0
|
CB
|
A:CYS1809
|
3.0
|
0.0
|
1.0
|
H
|
A:CYS1820
|
3.2
|
0.0
|
1.0
|
HA
|
A:LYS1812
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS1817
|
3.3
|
0.0
|
1.0
|
HB
|
A:VAL1819
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS1809
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS1817
|
3.3
|
0.0
|
1.0
|
CE1
|
A:HIS1805
|
3.3
|
0.0
|
1.0
|
H
|
A:LYS1812
|
3.5
|
0.0
|
1.0
|
HB2
|
A:CYS1817
|
3.6
|
0.0
|
1.0
|
HE1
|
A:HIS1805
|
3.8
|
0.0
|
1.0
|
CB
|
A:CYS1820
|
3.9
|
0.0
|
1.0
|
CG
|
A:HIS1805
|
4.1
|
0.0
|
1.0
|
HB2
|
A:CYS1820
|
4.1
|
0.0
|
1.0
|
N
|
A:CYS1820
|
4.1
|
0.0
|
1.0
|
CA
|
A:LYS1812
|
4.2
|
0.0
|
1.0
|
HA
|
A:THR1806
|
4.2
|
0.0
|
1.0
|
N
|
A:LYS1812
|
4.2
|
0.0
|
1.0
|
ND1
|
A:HIS1805
|
4.3
|
0.0
|
1.0
|
CB
|
A:VAL1819
|
4.4
|
0.0
|
1.0
|
HB3
|
A:LYS1812
|
4.4
|
0.0
|
1.0
|
HB3
|
A:ARG1811
|
4.4
|
0.0
|
1.0
|
CA
|
A:CYS1809
|
4.5
|
0.0
|
1.0
|
HA
|
A:CYS1809
|
4.6
|
0.0
|
1.0
|
H
|
A:VAL1819
|
4.6
|
0.0
|
1.0
|
CA
|
A:CYS1820
|
4.6
|
0.0
|
1.0
|
HB3
|
A:CYS1820
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS1817
|
4.7
|
0.0
|
1.0
|
HG13
|
A:VAL1819
|
4.8
|
0.0
|
1.0
|
CB
|
A:LYS1812
|
4.8
|
0.0
|
1.0
|
H
|
A:ARG1811
|
4.9
|
0.0
|
1.0
|
HA
|
A:CYS1820
|
4.9
|
0.0
|
1.0
|
|
Zinc binding site 3 out
of 3 in 2kje
Go back to
Zinc Binding Sites List in 2kje
Zinc binding site 3 out
of 3 in the uc(Nmr) Structure of Cbp TAZ2 and Adenoviral E1A Complex
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 Cbp TAZ2 and Adenoviral E1A Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn502
b:0.0
occ:1.00
|
NE2
|
A:HIS1830
|
2.1
|
0.0
|
1.0
|
SG
|
A:CYS1839
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS1844
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS1834
|
2.3
|
0.0
|
1.0
|
CD2
|
A:HIS1830
|
2.8
|
0.0
|
1.0
|
HD2
|
A:HIS1830
|
2.9
|
0.0
|
1.0
|
HB2
|
A:CYS1834
|
3.1
|
0.0
|
1.0
|
CB
|
A:CYS1834
|
3.1
|
0.0
|
1.0
|
HB3
|
A:CYS1834
|
3.3
|
0.0
|
1.0
|
CE1
|
A:HIS1830
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS1839
|
3.3
|
0.0
|
1.0
|
HB2
|
A:CYS1839
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS1839
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS1844
|
3.6
|
0.0
|
1.0
|
HB2
|
A:CYS1844
|
3.6
|
0.0
|
1.0
|
HE1
|
A:HIS1830
|
3.7
|
0.0
|
1.0
|
HB3
|
A:CYS1844
|
3.8
|
0.0
|
1.0
|
HE3
|
A:LYS1848
|
4.0
|
0.0
|
1.0
|
CG
|
A:HIS1830
|
4.1
|
0.0
|
1.0
|
HB
|
A:VAL1841
|
4.1
|
0.0
|
1.0
|
HA
|
A:ALA1831
|
4.1
|
0.0
|
1.0
|
HB3
|
A:GLU1836
|
4.2
|
0.0
|
1.0
|
ND1
|
A:HIS1830
|
4.3
|
0.0
|
1.0
|
HE2
|
A:LYS1848
|
4.4
|
0.0
|
1.0
|
H
|
A:GLU1836
|
4.6
|
0.0
|
1.0
|
CA
|
A:CYS1834
|
4.6
|
0.0
|
1.0
|
H
|
A:GLN1835
|
4.7
|
0.0
|
1.0
|
CE
|
A:LYS1848
|
4.7
|
0.0
|
1.0
|
HD3
|
A:LYS1848
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS1839
|
4.7
|
0.0
|
1.0
|
HA
|
A:CYS1834
|
4.8
|
0.0
|
1.0
|
CA
|
A:CYS1844
|
4.9
|
0.0
|
1.0
|
H
|
A:VAL1841
|
4.9
|
0.0
|
1.0
|
HA
|
A:CYS1839
|
4.9
|
0.0
|
1.0
|
HG21
|
A:VAL1841
|
5.0
|
0.0
|
1.0
|
HD2
|
A:PRO1840
|
5.0
|
0.0
|
1.0
|
HD21
|
A:LEU1845
|
5.0
|
0.0
|
1.0
|
|
Reference:
J.C.Ferreon,
M.A.Martinez-Yamout,
H.J.Dyson,
P.E.Wright.
Structural Basis For Subversion of Cellular Control Mechanisms By the Adenoviral E1A Oncoprotein. Proc.Natl.Acad.Sci.Usa V. 106 13260 2009.
ISSN: ISSN 0027-8424
PubMed: 19651603
DOI: 10.1073/PNAS.0906770106
Page generated: Thu Oct 17 01:36:08 2024
|