Zinc in PDB 3kds: Apo-Ftsh Crystal Structure
Protein crystallography data
The structure of Apo-Ftsh Crystal Structure, PDB code: 3kds
was solved by
C.Bieniossek,
B.Niederhauser,
U.Baumann,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
45.76 /
2.60
|
Space group
|
P 6 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
190.500,
190.500,
152.130,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
22.3 /
28.7
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Apo-Ftsh Crystal Structure
(pdb code 3kds). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Apo-Ftsh Crystal Structure, PDB code: 3kds:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 3kds
Go back to
Zinc Binding Sites List in 3kds
Zinc binding site 1 out
of 3 in the Apo-Ftsh Crystal Structure
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Apo-Ftsh Crystal Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn996
b:55.2
occ:1.00
|
NE2
|
E:HIS427
|
2.1
|
42.3
|
1.0
|
OD2
|
E:ASP500
|
2.1
|
61.0
|
1.0
|
NE2
|
E:HIS423
|
2.1
|
46.2
|
1.0
|
OAI
|
E:NHX998
|
2.1
|
59.8
|
1.0
|
OAF
|
E:NHX998
|
2.1
|
74.0
|
1.0
|
CG
|
E:ASP500
|
2.9
|
42.8
|
1.0
|
CAX
|
E:NHX998
|
2.9
|
59.9
|
1.0
|
OD1
|
E:ASP500
|
3.0
|
46.8
|
1.0
|
NAT
|
E:NHX998
|
3.0
|
55.4
|
1.0
|
CD2
|
E:HIS423
|
3.0
|
41.6
|
1.0
|
CE1
|
E:HIS423
|
3.1
|
48.7
|
1.0
|
CD2
|
E:HIS427
|
3.1
|
48.7
|
1.0
|
CE1
|
E:HIS427
|
3.1
|
42.9
|
1.0
|
ND1
|
E:HIS427
|
4.2
|
46.6
|
1.0
|
CG
|
E:HIS427
|
4.2
|
39.5
|
1.0
|
CG
|
E:HIS423
|
4.2
|
40.2
|
1.0
|
ND1
|
E:HIS423
|
4.2
|
37.7
|
1.0
|
OE2
|
E:GLU424
|
4.2
|
53.3
|
1.0
|
CB
|
E:ASP500
|
4.3
|
38.1
|
1.0
|
CAQ
|
E:NHX998
|
4.3
|
43.8
|
1.0
|
CAS
|
E:NHX998
|
4.6
|
54.0
|
1.0
|
CA
|
E:GLY482
|
4.7
|
37.6
|
1.0
|
CBF
|
E:NHX998
|
4.8
|
64.5
|
1.0
|
|
Zinc binding site 2 out
of 3 in 3kds
Go back to
Zinc Binding Sites List in 3kds
Zinc binding site 2 out
of 3 in the Apo-Ftsh Crystal Structure
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Apo-Ftsh Crystal Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Zn996
b:70.9
occ:1.00
|
NE2
|
F:HIS423
|
2.1
|
67.1
|
1.0
|
NE2
|
F:HIS427
|
2.1
|
62.7
|
1.0
|
OD2
|
F:ASP500
|
2.1
|
62.8
|
1.0
|
OAF
|
F:NHX998
|
2.1
|
65.1
|
1.0
|
OAI
|
F:NHX998
|
2.1
|
98.0
|
1.0
|
CAX
|
F:NHX998
|
2.8
|
75.3
|
1.0
|
NAT
|
F:NHX998
|
2.9
|
71.8
|
1.0
|
CD2
|
F:HIS423
|
3.0
|
61.1
|
1.0
|
CD2
|
F:HIS427
|
3.0
|
61.7
|
1.0
|
CG
|
F:ASP500
|
3.1
|
60.7
|
1.0
|
CE1
|
F:HIS427
|
3.1
|
56.5
|
1.0
|
CE1
|
F:HIS423
|
3.1
|
72.3
|
1.0
|
OD1
|
F:ASP500
|
3.4
|
73.1
|
1.0
|
OE2
|
F:GLU424
|
4.1
|
75.2
|
1.0
|
CG
|
F:HIS423
|
4.1
|
63.2
|
1.0
|
ND1
|
F:HIS427
|
4.2
|
74.9
|
1.0
|
CG
|
F:HIS427
|
4.2
|
66.4
|
1.0
|
ND1
|
F:HIS423
|
4.2
|
68.9
|
1.0
|
CAQ
|
F:NHX998
|
4.3
|
85.7
|
1.0
|
CAS
|
F:NHX998
|
4.4
|
82.4
|
1.0
|
CB
|
F:ASP500
|
4.4
|
46.3
|
1.0
|
CA
|
F:GLY482
|
4.5
|
59.6
|
1.0
|
CBF
|
F:NHX998
|
4.7
|
0.5
|
1.0
|
CD
|
F:GLU424
|
5.0
|
75.5
|
1.0
|
|
Zinc binding site 3 out
of 3 in 3kds
Go back to
Zinc Binding Sites List in 3kds
Zinc binding site 3 out
of 3 in the Apo-Ftsh Crystal Structure
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Apo-Ftsh Crystal Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Zn996
b:65.4
occ:1.00
|
NE2
|
G:HIS423
|
2.1
|
63.0
|
1.0
|
OD2
|
G:ASP500
|
2.1
|
65.4
|
1.0
|
OAF
|
G:NHX998
|
2.1
|
76.9
|
1.0
|
NE2
|
G:HIS427
|
2.1
|
55.3
|
1.0
|
OAI
|
G:NHX998
|
2.1
|
81.4
|
1.0
|
CAX
|
G:NHX998
|
2.8
|
61.8
|
1.0
|
NAT
|
G:NHX998
|
2.9
|
63.8
|
1.0
|
CD2
|
G:HIS427
|
3.0
|
68.2
|
1.0
|
CD2
|
G:HIS423
|
3.0
|
61.5
|
1.0
|
CG
|
G:ASP500
|
3.0
|
59.1
|
1.0
|
CE1
|
G:HIS423
|
3.1
|
72.4
|
1.0
|
CE1
|
G:HIS427
|
3.2
|
47.9
|
1.0
|
OD1
|
G:ASP500
|
3.3
|
68.8
|
1.0
|
OE2
|
G:GLU424
|
4.0
|
75.9
|
1.0
|
CG
|
G:HIS427
|
4.2
|
59.2
|
1.0
|
CG
|
G:HIS423
|
4.2
|
64.1
|
1.0
|
ND1
|
G:HIS423
|
4.2
|
65.9
|
1.0
|
ND1
|
G:HIS427
|
4.2
|
72.7
|
1.0
|
CAQ
|
G:NHX998
|
4.3
|
53.0
|
1.0
|
CB
|
G:ASP500
|
4.4
|
47.3
|
1.0
|
CAS
|
G:NHX998
|
4.5
|
69.5
|
1.0
|
CA
|
G:GLY482
|
4.6
|
56.7
|
1.0
|
CBF
|
G:NHX998
|
4.7
|
73.8
|
1.0
|
CD
|
G:GLU424
|
4.9
|
78.1
|
1.0
|
OE1
|
G:GLU424
|
4.9
|
74.9
|
1.0
|
|
Reference:
C.Bieniossek,
B.Niederhauser,
U.M.Baumann.
The Crystal Structure of Apo-Ftsh Reveals Domain Movements Necessary For Substrate Unfolding and Translocation Proc.Natl.Acad.Sci.Usa V. 106 21579 2009.
ISSN: ISSN 0027-8424
PubMed: 19955424
DOI: 10.1073/PNAS.0910708106
Page generated: Sat Oct 26 07:45:57 2024
|