Zinc in PDB 5n12: Crystal Structure of Tce Treated Rppep-1
Enzymatic activity of Crystal Structure of Tce Treated Rppep-1
All present enzymatic activity of Crystal Structure of Tce Treated Rppep-1:
3.4.24.89;
Protein crystallography data
The structure of Crystal Structure of Tce Treated Rppep-1, PDB code: 5n12
was solved by
C.Pichlo,
M.Schacherl,
U.Baumann,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
45.53 /
1.38
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
43.169,
71.769,
117.798,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.4 /
18.4
|
Other elements in 5n12:
The structure of Crystal Structure of Tce Treated Rppep-1 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Tce Treated Rppep-1
(pdb code 5n12). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Crystal Structure of Tce Treated Rppep-1, PDB code: 5n12:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 5n12
Go back to
Zinc Binding Sites List in 5n12
Zinc binding site 1 out
of 2 in the Crystal Structure of Tce Treated Rppep-1
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of Tce Treated Rppep-1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:14.1
occ:1.00
|
OE1
|
A:GLU185
|
2.1
|
12.1
|
1.0
|
NE2
|
A:HIS142
|
2.1
|
11.2
|
1.0
|
NE2
|
A:HIS146
|
2.1
|
11.3
|
1.0
|
N
|
A:TRS303
|
2.1
|
16.1
|
1.0
|
O2
|
A:TRS303
|
2.2
|
16.0
|
1.0
|
O3
|
A:TRS303
|
2.3
|
18.1
|
1.0
|
HO3
|
A:TRS303
|
2.4
|
21.8
|
1.0
|
HO2
|
A:TRS303
|
2.5
|
19.2
|
1.0
|
HN1
|
A:TRS303
|
2.5
|
19.3
|
1.0
|
HN2
|
A:TRS303
|
2.6
|
19.3
|
1.0
|
C
|
A:TRS303
|
2.9
|
16.5
|
1.0
|
CD
|
A:GLU185
|
3.0
|
13.5
|
1.0
|
C2
|
A:TRS303
|
3.0
|
15.8
|
1.0
|
CD2
|
A:HIS142
|
3.0
|
11.6
|
1.0
|
CD2
|
A:HIS146
|
3.1
|
10.6
|
1.0
|
CE1
|
A:HIS146
|
3.1
|
11.9
|
1.0
|
CE1
|
A:HIS142
|
3.1
|
10.4
|
1.0
|
C3
|
A:TRS303
|
3.1
|
17.8
|
1.0
|
OE2
|
A:GLU185
|
3.2
|
14.1
|
1.0
|
HD2
|
A:HIS142
|
3.2
|
14.0
|
1.0
|
HD2
|
A:HIS146
|
3.2
|
12.8
|
1.0
|
HE1
|
A:HIS146
|
3.3
|
14.3
|
1.0
|
HE1
|
A:HIS142
|
3.3
|
12.4
|
1.0
|
H22
|
A:TRS303
|
3.4
|
18.9
|
1.0
|
H32
|
A:TRS303
|
3.7
|
21.4
|
1.0
|
H31
|
A:TRS303
|
3.8
|
21.4
|
1.0
|
H21
|
A:TRS303
|
3.9
|
18.9
|
1.0
|
HA
|
A:GLU185
|
4.1
|
13.1
|
1.0
|
ND1
|
A:HIS146
|
4.2
|
11.7
|
1.0
|
ND1
|
A:HIS142
|
4.2
|
10.8
|
1.0
|
CG
|
A:HIS142
|
4.2
|
11.2
|
1.0
|
OH
|
A:TYR178
|
4.2
|
16.8
|
1.0
|
CG
|
A:HIS146
|
4.2
|
10.8
|
1.0
|
O
|
A:HOH501
|
4.2
|
19.5
|
1.0
|
OE1
|
A:GLU143
|
4.3
|
13.0
|
1.0
|
HB3
|
A:ALA188
|
4.3
|
14.5
|
1.0
|
O
|
A:HOH578
|
4.3
|
13.5
|
1.0
|
C1
|
A:TRS303
|
4.3
|
18.0
|
1.0
|
CG
|
A:GLU185
|
4.4
|
13.0
|
1.0
|
HE2
|
A:TYR178
|
4.4
|
21.0
|
1.0
|
HB3
|
A:GLU185
|
4.5
|
13.9
|
1.0
|
H11
|
A:TRS303
|
4.6
|
21.6
|
1.0
|
HH
|
A:TYR178
|
4.7
|
20.1
|
1.0
|
HB1
|
A:ALA188
|
4.8
|
14.5
|
1.0
|
HG3
|
A:GLU185
|
4.8
|
15.7
|
1.0
|
CB
|
A:GLU185
|
4.8
|
11.6
|
1.0
|
CB
|
A:ALA188
|
4.8
|
12.1
|
1.0
|
OE2
|
A:GLU143
|
4.9
|
17.5
|
1.0
|
HB2
|
A:ALA188
|
4.9
|
14.5
|
1.0
|
H12
|
A:TRS303
|
4.9
|
21.6
|
1.0
|
CA
|
A:GLU185
|
4.9
|
10.9
|
1.0
|
HG2
|
A:GLU185
|
5.0
|
15.7
|
1.0
|
HD1
|
A:HIS146
|
5.0
|
14.0
|
1.0
|
CD
|
A:GLU143
|
5.0
|
14.0
|
1.0
|
O1
|
A:TRS303
|
5.0
|
16.9
|
1.0
|
HD1
|
A:HIS142
|
5.0
|
13.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 5n12
Go back to
Zinc Binding Sites List in 5n12
Zinc binding site 2 out
of 2 in the Crystal Structure of Tce Treated Rppep-1
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of Tce Treated Rppep-1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn301
b:13.8
occ:1.00
|
HO2
|
B:TRS304
|
1.6
|
30.3
|
1.0
|
HO3
|
B:TRS304
|
2.0
|
28.1
|
1.0
|
OE1
|
B:GLU185
|
2.0
|
14.9
|
1.0
|
NE2
|
B:HIS146
|
2.1
|
11.1
|
1.0
|
NE2
|
B:HIS142
|
2.1
|
11.9
|
1.0
|
N
|
B:TRS304
|
2.1
|
25.7
|
1.0
|
O2
|
B:TRS304
|
2.2
|
25.2
|
1.0
|
O3
|
B:TRS304
|
2.4
|
23.5
|
1.0
|
HN2
|
B:TRS304
|
2.5
|
30.9
|
1.0
|
HN1
|
B:TRS304
|
2.6
|
30.9
|
1.0
|
C
|
B:TRS304
|
2.9
|
27.6
|
1.0
|
CD
|
B:GLU185
|
2.9
|
14.8
|
1.0
|
CE1
|
B:HIS146
|
3.0
|
11.3
|
1.0
|
CD2
|
B:HIS142
|
3.0
|
10.8
|
1.0
|
C2
|
B:TRS304
|
3.0
|
27.1
|
1.0
|
CE1
|
B:HIS142
|
3.1
|
11.5
|
1.0
|
CD2
|
B:HIS146
|
3.1
|
11.2
|
1.0
|
HE1
|
B:HIS146
|
3.2
|
13.6
|
1.0
|
HD2
|
B:HIS142
|
3.2
|
13.0
|
1.0
|
OE2
|
B:GLU185
|
3.2
|
16.7
|
1.0
|
C3
|
B:TRS304
|
3.2
|
24.7
|
1.0
|
HE1
|
B:HIS142
|
3.3
|
13.8
|
1.0
|
HD2
|
B:HIS146
|
3.3
|
13.5
|
1.0
|
H22
|
B:TRS304
|
3.5
|
32.5
|
1.0
|
H32
|
B:TRS304
|
3.8
|
29.6
|
1.0
|
H21
|
B:TRS304
|
3.8
|
32.5
|
1.0
|
H31
|
B:TRS304
|
3.9
|
29.6
|
1.0
|
HA
|
B:GLU185
|
4.0
|
14.1
|
1.0
|
ND1
|
B:HIS146
|
4.1
|
12.0
|
1.0
|
HB3
|
B:ALA188
|
4.2
|
14.5
|
1.0
|
ND1
|
B:HIS142
|
4.2
|
11.7
|
1.0
|
CG
|
B:HIS142
|
4.2
|
11.2
|
1.0
|
CG
|
B:HIS146
|
4.2
|
10.8
|
1.0
|
OE1
|
B:GLU143
|
4.2
|
14.0
|
1.0
|
C1
|
B:TRS304
|
4.3
|
32.0
|
1.0
|
CG
|
B:GLU185
|
4.3
|
13.2
|
1.0
|
O
|
B:HOH566
|
4.3
|
17.8
|
1.0
|
OH
|
B:TYR178
|
4.4
|
20.4
|
1.0
|
O
|
B:HOH534
|
4.4
|
18.8
|
1.0
|
HE2
|
B:TYR178
|
4.4
|
22.9
|
1.0
|
HB3
|
B:GLU185
|
4.5
|
15.0
|
1.0
|
H11
|
B:TRS304
|
4.5
|
38.4
|
1.0
|
H12
|
B:TRS304
|
4.6
|
38.4
|
1.0
|
HB1
|
B:ALA188
|
4.7
|
14.5
|
1.0
|
HG3
|
B:GLU185
|
4.7
|
15.9
|
1.0
|
CB
|
B:ALA188
|
4.8
|
12.1
|
1.0
|
CB
|
B:GLU185
|
4.8
|
12.5
|
1.0
|
OE2
|
B:GLU143
|
4.8
|
20.5
|
1.0
|
CA
|
B:GLU185
|
4.8
|
11.8
|
1.0
|
HB2
|
B:ALA188
|
4.8
|
14.5
|
1.0
|
HH
|
B:TYR178
|
4.9
|
24.4
|
1.0
|
HG2
|
B:GLU185
|
4.9
|
15.9
|
1.0
|
CD
|
B:GLU143
|
4.9
|
15.6
|
1.0
|
HD1
|
B:HIS146
|
4.9
|
14.3
|
1.0
|
HD1
|
B:HIS142
|
5.0
|
14.0
|
1.0
|
|
Reference:
C.Pichlo,
C.Toelzer,
K.Chojnacki,
S.Ocal,
M.Uthoff,
S.Ruegenberg,
T.Hermanns,
M.Schacherl,
M.S.Denzel,
K.Hofmann,
K.Niefind,
U.Baumann.
Improved Protein-Crystal Identification By Using 2,2,2-Trichloroethanol As A Fluorescence Enhancer. Acta Crystallogr F Struct V. 74 307 2018BIOL Commun.
ISSN: ESSN 2053-230X
PubMed: 29717999
DOI: 10.1107/S2053230X18005253
Page generated: Sun Oct 27 22:27:05 2024
|