Zinc in PDB 4nt9: Crystal Structure of An L,D-Carboxypeptidase Dacb From Streptococcus Pneumonia
Protein crystallography data
The structure of Crystal Structure of An L,D-Carboxypeptidase Dacb From Streptococcus Pneumonia, PDB code: 4nt9
was solved by
Y.H.Yang,
J.Zhang,
Y.L.Jiang,
C.Z.Zhou,
Y.Chen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
41.47 /
1.71
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
55.110,
68.080,
80.350,
90.00,
108.41,
90.00
|
R / Rfree (%)
|
17.7 /
21.2
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of An L,D-Carboxypeptidase Dacb From Streptococcus Pneumonia
(pdb code 4nt9). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Crystal Structure of An L,D-Carboxypeptidase Dacb From Streptococcus Pneumonia, PDB code: 4nt9:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 4nt9
Go back to
Zinc Binding Sites List in 4nt9
Zinc binding site 1 out
of 3 in the Crystal Structure of An L,D-Carboxypeptidase Dacb From Streptococcus Pneumonia
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 An L,D-Carboxypeptidase Dacb From Streptococcus Pneumonia within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn301
b:16.2
occ:1.00
|
O
|
B:HOH406
|
2.0
|
13.4
|
1.0
|
ND1
|
B:HIS207
|
2.0
|
13.0
|
1.0
|
OD1
|
B:ASP160
|
2.1
|
14.5
|
1.0
|
NE2
|
B:HIS153
|
2.1
|
13.4
|
1.0
|
O
|
B:HOH416
|
2.1
|
14.5
|
1.0
|
OE1
|
B:GLU204
|
2.2
|
17.4
|
1.0
|
CE1
|
B:HIS207
|
2.9
|
12.9
|
1.0
|
CE1
|
B:HIS153
|
3.1
|
12.6
|
1.0
|
CG
|
B:ASP160
|
3.1
|
15.5
|
1.0
|
CD2
|
B:HIS153
|
3.1
|
12.5
|
1.0
|
CG
|
B:HIS207
|
3.1
|
11.8
|
1.0
|
CD
|
B:GLU204
|
3.2
|
14.6
|
1.0
|
OD2
|
B:ASP160
|
3.4
|
15.9
|
1.0
|
OE2
|
B:GLU204
|
3.5
|
18.2
|
1.0
|
CB
|
B:HIS207
|
3.6
|
11.6
|
1.0
|
NE2
|
B:HIS207
|
4.1
|
13.7
|
1.0
|
O1
|
B:GOL303
|
4.2
|
24.1
|
1.0
|
NE1
|
B:TRP206
|
4.2
|
17.2
|
1.0
|
CD2
|
B:HIS207
|
4.2
|
13.1
|
1.0
|
ND1
|
B:HIS153
|
4.2
|
13.1
|
1.0
|
OXT
|
B:ACT302
|
4.2
|
18.6
|
1.0
|
CG
|
B:HIS153
|
4.3
|
12.5
|
1.0
|
NH1
|
B:ARG120
|
4.3
|
21.0
|
1.0
|
CB
|
B:ASP160
|
4.5
|
16.9
|
1.0
|
CD1
|
B:TRP206
|
4.6
|
15.7
|
1.0
|
CG
|
B:GLU204
|
4.6
|
16.4
|
1.0
|
CA
|
B:HIS207
|
4.7
|
10.8
|
1.0
|
C
|
B:ACT302
|
4.8
|
20.8
|
1.0
|
NH2
|
B:ARG120
|
4.9
|
18.9
|
1.0
|
CE2
|
B:TYR191
|
4.9
|
13.3
|
1.0
|
CA
|
B:ASP160
|
5.0
|
13.4
|
1.0
|
CH3
|
B:ACT302
|
5.0
|
23.4
|
1.0
|
|
Zinc binding site 2 out
of 3 in 4nt9
Go back to
Zinc Binding Sites List in 4nt9
Zinc binding site 2 out
of 3 in the Crystal Structure of An L,D-Carboxypeptidase Dacb From Streptococcus Pneumonia
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 An L,D-Carboxypeptidase Dacb From Streptococcus Pneumonia within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:18.6
occ:1.00
|
ND1
|
A:HIS207
|
2.0
|
14.5
|
1.0
|
OD1
|
A:ASP160
|
2.1
|
17.4
|
1.0
|
NE2
|
A:HIS153
|
2.1
|
15.3
|
1.0
|
O
|
A:HOH413
|
2.1
|
18.1
|
1.0
|
O
|
A:HOH434
|
2.2
|
17.8
|
1.0
|
OE1
|
A:GLU204
|
2.3
|
18.1
|
1.0
|
CE1
|
A:HIS207
|
2.9
|
13.5
|
1.0
|
CG
|
A:ASP160
|
3.0
|
16.5
|
1.0
|
CD2
|
A:HIS153
|
3.1
|
15.9
|
1.0
|
CE1
|
A:HIS153
|
3.1
|
15.7
|
1.0
|
CG
|
A:HIS207
|
3.2
|
13.6
|
1.0
|
OD2
|
A:ASP160
|
3.2
|
17.7
|
1.0
|
CD
|
A:GLU204
|
3.3
|
16.9
|
1.0
|
OE2
|
A:GLU204
|
3.6
|
18.0
|
1.0
|
CB
|
A:HIS207
|
3.6
|
13.6
|
1.0
|
NE2
|
A:HIS207
|
4.0
|
13.2
|
1.0
|
CD2
|
A:HIS207
|
4.2
|
13.5
|
1.0
|
ND1
|
A:HIS153
|
4.2
|
16.9
|
1.0
|
NE1
|
A:TRP206
|
4.2
|
19.6
|
1.0
|
CG
|
A:HIS153
|
4.2
|
15.3
|
1.0
|
O
|
A:ACT302
|
4.3
|
22.2
|
1.0
|
O
|
A:HOH476
|
4.4
|
26.1
|
1.0
|
NH1
|
A:ARG120
|
4.4
|
26.9
|
1.0
|
CB
|
A:ASP160
|
4.5
|
17.1
|
1.0
|
CD1
|
A:TRP206
|
4.6
|
16.2
|
1.0
|
CA
|
A:HIS207
|
4.7
|
13.6
|
1.0
|
CG
|
A:GLU204
|
4.7
|
15.1
|
1.0
|
NH2
|
A:ARG120
|
4.9
|
23.8
|
1.0
|
CE2
|
A:TYR191
|
4.9
|
15.0
|
1.0
|
CA
|
A:ASP160
|
5.0
|
16.5
|
1.0
|
C
|
A:ACT302
|
5.0
|
25.2
|
1.0
|
|
Zinc binding site 3 out
of 3 in 4nt9
Go back to
Zinc Binding Sites List in 4nt9
Zinc binding site 3 out
of 3 in the Crystal Structure of An L,D-Carboxypeptidase Dacb From Streptococcus Pneumonia
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of An L,D-Carboxypeptidase Dacb From Streptococcus Pneumonia within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn301
b:18.6
occ:1.00
|
ND1
|
C:HIS207
|
2.0
|
15.2
|
1.0
|
OD1
|
C:ASP160
|
2.1
|
15.8
|
1.0
|
O
|
C:HOH413
|
2.1
|
18.8
|
1.0
|
NE2
|
C:HIS153
|
2.1
|
17.3
|
1.0
|
O
|
C:HOH430
|
2.2
|
18.6
|
1.0
|
OE1
|
C:GLU204
|
2.3
|
20.1
|
1.0
|
CE1
|
C:HIS207
|
2.9
|
16.2
|
1.0
|
CG
|
C:ASP160
|
3.1
|
17.5
|
1.0
|
CG
|
C:HIS207
|
3.1
|
13.1
|
1.0
|
CE1
|
C:HIS153
|
3.1
|
16.7
|
1.0
|
CD2
|
C:HIS153
|
3.2
|
16.2
|
1.0
|
CD
|
C:GLU204
|
3.2
|
17.7
|
1.0
|
OD2
|
C:ASP160
|
3.3
|
17.4
|
1.0
|
OE2
|
C:GLU204
|
3.4
|
17.1
|
1.0
|
CB
|
C:HIS207
|
3.5
|
12.3
|
1.0
|
NE2
|
C:HIS207
|
4.0
|
15.8
|
1.0
|
CD2
|
C:HIS207
|
4.2
|
15.8
|
1.0
|
NE1
|
C:TRP206
|
4.2
|
17.5
|
1.0
|
ND1
|
C:HIS153
|
4.2
|
19.1
|
1.0
|
O
|
C:HOH431
|
4.3
|
21.0
|
1.0
|
CG
|
C:HIS153
|
4.3
|
17.9
|
1.0
|
O
|
C:ACT302
|
4.3
|
21.5
|
1.0
|
NH1
|
C:ARG120
|
4.4
|
22.1
|
1.0
|
CB
|
C:ASP160
|
4.5
|
16.7
|
1.0
|
CA
|
C:HIS207
|
4.6
|
13.4
|
1.0
|
CD1
|
C:TRP206
|
4.6
|
17.7
|
1.0
|
CG
|
C:GLU204
|
4.6
|
17.1
|
1.0
|
NH2
|
C:ARG120
|
4.8
|
21.8
|
1.0
|
CE2
|
C:TYR191
|
4.9
|
15.4
|
1.0
|
C
|
C:ACT302
|
4.9
|
22.1
|
1.0
|
|
Reference:
Y.H.Yang,
J.Zhang,
Y.L.Jiang,
C.Z.Zhou,
Y.Chen.
Crystal Structure of An L,D-Carboxypeptidase Dacb From Streptococcus Pneumonia To Be Published.
Page generated: Sun Oct 27 03:20:15 2024
|