Zinc in PDB 7c4c: The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex
Protein crystallography data
The structure of The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex, PDB code: 7c4c
was solved by
Y.Q.Gao,
J.H.Gan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
2.27
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
57.169,
75.001,
101.409,
90,
90,
90
|
R / Rfree (%)
|
19.2 /
23.9
|
Other elements in 7c4c:
The structure of The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex
(pdb code 7c4c). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex, PDB code: 7c4c:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 7c4c
Go back to
Zinc Binding Sites List in 7c4c
Zinc binding site 1 out
of 6 in the The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn401
b:34.2
occ:1.00
|
NE2
|
A:HIS328
|
2.2
|
46.0
|
1.0
|
SG
|
A:CYS333
|
2.2
|
28.8
|
1.0
|
SG
|
A:CYS320
|
2.2
|
31.4
|
1.0
|
SG
|
A:CYS323
|
2.3
|
37.9
|
1.0
|
CB
|
A:CYS333
|
2.9
|
32.1
|
1.0
|
CD2
|
A:HIS328
|
3.0
|
45.8
|
1.0
|
CB
|
A:CYS320
|
3.1
|
33.1
|
1.0
|
CE1
|
A:HIS328
|
3.3
|
48.5
|
1.0
|
CB
|
A:CYS323
|
3.3
|
38.1
|
1.0
|
O6
|
A:5GP414
|
3.7
|
58.0
|
1.0
|
N
|
A:CYS323
|
3.8
|
38.3
|
1.0
|
CA
|
A:CYS333
|
3.8
|
31.2
|
1.0
|
CA
|
A:CYS323
|
4.1
|
40.5
|
1.0
|
CG
|
A:HIS328
|
4.2
|
46.8
|
1.0
|
ND1
|
A:HIS328
|
4.3
|
50.1
|
1.0
|
CA
|
A:CYS320
|
4.5
|
35.1
|
1.0
|
C6
|
A:5GP414
|
4.7
|
65.2
|
1.0
|
C
|
A:CYS333
|
4.7
|
31.1
|
1.0
|
C
|
A:CYS323
|
4.8
|
43.2
|
1.0
|
C
|
A:PHE322
|
4.8
|
38.6
|
1.0
|
CB
|
A:PHE322
|
4.8
|
27.3
|
1.0
|
N
|
A:PHE334
|
4.8
|
30.3
|
1.0
|
O
|
A:THR329
|
4.9
|
39.8
|
1.0
|
N
|
A:CYS333
|
4.9
|
37.6
|
1.0
|
N
|
A:GLY324
|
5.0
|
42.4
|
1.0
|
|
Zinc binding site 2 out
of 6 in 7c4c
Go back to
Zinc Binding Sites List in 7c4c
Zinc binding site 2 out
of 6 in the The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn402
b:26.6
occ:1.00
|
NE2
|
A:HIS305
|
2.1
|
34.4
|
1.0
|
SG
|
A:CYS300
|
2.2
|
28.0
|
1.0
|
SG
|
A:CYS310
|
2.3
|
25.1
|
1.0
|
SG
|
A:CYS297
|
2.3
|
26.5
|
1.0
|
CB
|
A:CYS310
|
3.0
|
26.9
|
1.0
|
CE1
|
A:HIS305
|
3.0
|
30.6
|
1.0
|
CB
|
A:CYS297
|
3.1
|
25.4
|
1.0
|
CD2
|
A:HIS305
|
3.1
|
35.7
|
1.0
|
CB
|
A:CYS300
|
3.2
|
26.9
|
1.0
|
N
|
A:CYS300
|
3.7
|
31.4
|
1.0
|
CA
|
A:CYS310
|
3.9
|
34.3
|
1.0
|
CA
|
A:CYS300
|
4.0
|
30.1
|
1.0
|
ND1
|
A:HIS305
|
4.1
|
28.9
|
1.0
|
CG
|
A:HIS305
|
4.2
|
28.4
|
1.0
|
O6
|
A:5GP416
|
4.5
|
71.6
|
1.0
|
CA
|
A:CYS297
|
4.6
|
22.7
|
1.0
|
CB
|
A:PHE299
|
4.7
|
23.8
|
1.0
|
C
|
A:CYS300
|
4.8
|
27.4
|
1.0
|
C
|
A:PHE299
|
4.8
|
30.2
|
1.0
|
N
|
A:GLY301
|
4.8
|
25.5
|
1.0
|
C
|
A:CYS310
|
4.9
|
41.6
|
1.0
|
N
|
A:CYS310
|
4.9
|
29.0
|
1.0
|
O
|
A:THR306
|
5.0
|
28.2
|
1.0
|
|
Zinc binding site 3 out
of 6 in 7c4c
Go back to
Zinc Binding Sites List in 7c4c
Zinc binding site 3 out
of 6 in the The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn403
b:78.9
occ:1.00
|
NZ
|
A:LYS65
|
2.0
|
81.9
|
1.0
|
NE2
|
A:HIS61
|
2.4
|
40.6
|
1.0
|
OD1
|
A:ASP125
|
2.7
|
54.6
|
1.0
|
CE
|
A:LYS65
|
2.9
|
75.7
|
1.0
|
OD2
|
A:ASP125
|
3.0
|
57.1
|
1.0
|
CE1
|
A:HIS61
|
3.1
|
46.3
|
1.0
|
CG
|
A:ASP125
|
3.2
|
51.4
|
1.0
|
CD2
|
A:HIS61
|
3.5
|
40.2
|
1.0
|
CD
|
A:LYS65
|
4.3
|
67.0
|
1.0
|
ND1
|
A:HIS61
|
4.3
|
50.9
|
1.0
|
CG
|
A:HIS61
|
4.5
|
41.6
|
1.0
|
CB
|
A:ASP125
|
4.7
|
41.8
|
1.0
|
CG
|
A:LYS65
|
4.8
|
56.0
|
1.0
|
|
Zinc binding site 4 out
of 6 in 7c4c
Go back to
Zinc Binding Sites List in 7c4c
Zinc binding site 4 out
of 6 in the The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn404
b:45.0
occ:1.00
|
OE2
|
A:GLU197
|
2.2
|
48.0
|
1.0
|
NE2
|
A:HIS233
|
2.3
|
34.8
|
1.0
|
O
|
A:HOH539
|
2.3
|
18.8
|
1.0
|
CE1
|
A:HIS233
|
3.0
|
37.8
|
1.0
|
CD
|
A:GLU197
|
3.2
|
46.4
|
1.0
|
CD2
|
A:HIS233
|
3.3
|
30.2
|
1.0
|
OE1
|
A:GLU197
|
3.5
|
44.6
|
1.0
|
ND1
|
A:HIS233
|
4.1
|
36.8
|
1.0
|
CA
|
A:GLY229
|
4.2
|
25.1
|
1.0
|
CD2
|
A:LEU51
|
4.3
|
39.6
|
1.0
|
CG
|
A:HIS233
|
4.3
|
33.1
|
1.0
|
O
|
A:GLY229
|
4.5
|
26.4
|
1.0
|
CG
|
A:GLU197
|
4.5
|
44.1
|
1.0
|
C
|
A:GLY229
|
4.7
|
23.2
|
1.0
|
|
Zinc binding site 5 out
of 6 in 7c4c
Go back to
Zinc Binding Sites List in 7c4c
Zinc binding site 5 out
of 6 in the The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn405
b:64.4
occ:1.00
|
SG
|
A:CYS374
|
2.3
|
62.9
|
1.0
|
SG
|
A:CYS365
|
2.5
|
67.7
|
1.0
|
SG
|
A:CYS362
|
2.7
|
76.7
|
1.0
|
NE2
|
A:HIS369
|
2.7
|
72.8
|
1.0
|
CB
|
A:CYS374
|
3.0
|
67.2
|
1.0
|
CE1
|
A:HIS369
|
3.3
|
73.3
|
1.0
|
CB
|
A:CYS362
|
3.4
|
80.3
|
1.0
|
CB
|
A:CYS365
|
3.7
|
67.3
|
1.0
|
CD2
|
A:HIS369
|
3.8
|
71.7
|
1.0
|
CA
|
A:CYS374
|
3.9
|
71.5
|
1.0
|
N
|
A:CYS365
|
4.0
|
74.2
|
1.0
|
CB
|
A:HIS364
|
4.4
|
96.4
|
1.0
|
ND1
|
A:HIS369
|
4.4
|
73.2
|
1.0
|
CA
|
A:CYS365
|
4.5
|
66.9
|
1.0
|
CG
|
A:HIS369
|
4.7
|
73.0
|
1.0
|
C
|
A:HIS364
|
4.8
|
82.8
|
1.0
|
CA
|
A:HIS364
|
4.8
|
89.1
|
1.0
|
N
|
A:GLY367
|
4.9
|
59.3
|
1.0
|
N
|
A:CYS374
|
4.9
|
79.8
|
1.0
|
C
|
A:CYS374
|
4.9
|
66.6
|
1.0
|
CD
|
A:LYS376
|
4.9
|
58.5
|
1.0
|
CA
|
A:CYS362
|
4.9
|
81.8
|
1.0
|
N
|
A:HIS364
|
4.9
|
88.9
|
1.0
|
|
Zinc binding site 6 out
of 6 in 7c4c
Go back to
Zinc Binding Sites List in 7c4c
Zinc binding site 6 out
of 6 in the The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of The Crystal Structure of Trypanosoma Brucei Rnase D : Gmp Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn406
b:125.3
occ:1.00
|
SG
|
A:CYS343
|
2.3
|
165.7
|
1.0
|
SG
|
A:CYS356
|
2.3
|
105.7
|
1.0
|
SG
|
A:CYS346
|
2.7
|
103.8
|
1.0
|
CD2
|
A:HIS351
|
2.9
|
89.4
|
1.0
|
NE2
|
A:HIS351
|
3.0
|
90.1
|
1.0
|
CB
|
A:CYS356
|
3.3
|
101.4
|
1.0
|
CB
|
A:CYS346
|
3.6
|
107.6
|
1.0
|
CB
|
A:CYS343
|
3.6
|
157.4
|
1.0
|
CA
|
A:CYS356
|
4.0
|
98.3
|
1.0
|
CG
|
A:HIS351
|
4.2
|
89.6
|
1.0
|
N
|
A:CYS346
|
4.2
|
94.7
|
1.0
|
O
|
A:THR352
|
4.2
|
121.2
|
1.0
|
CE1
|
A:HIS351
|
4.3
|
89.2
|
1.0
|
CA
|
A:CYS346
|
4.5
|
109.1
|
1.0
|
C
|
A:LYS345
|
4.7
|
92.0
|
1.0
|
ND1
|
A:HIS351
|
4.9
|
89.3
|
1.0
|
N
|
A:LYS345
|
4.9
|
100.8
|
1.0
|
N
|
A:CYS356
|
4.9
|
95.5
|
1.0
|
CA
|
A:CYS343
|
4.9
|
143.3
|
1.0
|
O
|
A:HIS351
|
5.0
|
102.5
|
1.0
|
O
|
A:CYS356
|
5.0
|
103.5
|
1.0
|
|
Reference:
Y.Gao,
H.Liu,
C.Zhang,
S.Su,
Y.Chen,
X.Chen,
Y.Li,
Z.Shao,
Y.Zhang,
Q.Shao,
J.Li,
Z.Huang,
J.Ma,
J.Gan.
Structural Basis For Guide Rna Trimming By Rnase D Ribonuclease in Trypanosoma Brucei. Nucleic Acids Res. V. 49 568 2021.
ISSN: ESSN 1362-4962
PubMed: 33332555
DOI: 10.1093/NAR/GKAA1197
Page generated: Tue Oct 29 18:04:06 2024
|