Sodium in PDB 6c5b: Crystal Structure Analysis of Laphzm
Protein crystallography data
The structure of Crystal Structure Analysis of Laphzm, PDB code: 6c5b
was solved by
D.G.Beltran,
A.Schacht,
L.Zhang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
71.42 /
1.42
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
56.275,
81.017,
72.164,
90.00,
98.23,
90.00
|
R / Rfree (%)
|
18.1 /
20.3
|
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure Analysis of Laphzm
(pdb code 6c5b). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the
Crystal Structure Analysis of Laphzm, PDB code: 6c5b:
Jump to Sodium binding site number:
1;
2;
3;
Sodium binding site 1 out
of 3 in 6c5b
Go back to
Sodium Binding Sites List in 6c5b
Sodium binding site 1 out
of 3 in the Crystal Structure Analysis of Laphzm
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Crystal Structure Analysis of Laphzm within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na504
b:32.4
occ:0.50
|
NH1
|
B:ARG67
|
0.7
|
15.1
|
0.5
|
CZ
|
B:ARG67
|
2.0
|
17.6
|
0.5
|
OG1
|
B:THR68
|
2.6
|
13.3
|
1.0
|
OD2
|
A:ASP295
|
2.8
|
16.5
|
1.0
|
NH2
|
B:ARG67
|
2.8
|
17.3
|
0.5
|
O
|
A:LYS292
|
2.9
|
12.4
|
1.0
|
NE
|
B:ARG67
|
3.0
|
16.3
|
0.5
|
O
|
B:HOH501
|
3.1
|
17.9
|
0.5
|
O
|
B:ARG64
|
3.2
|
11.0
|
1.0
|
CD
|
B:ARG67
|
3.4
|
17.0
|
0.5
|
CG
|
A:ASP295
|
3.6
|
13.4
|
1.0
|
C
|
B:ARG64
|
3.7
|
9.9
|
1.0
|
CB
|
B:ARG64
|
3.7
|
11.5
|
1.0
|
CD2
|
A:LEU296
|
3.8
|
12.6
|
1.0
|
CB
|
A:ASP295
|
3.8
|
13.4
|
1.0
|
C
|
A:LYS292
|
3.8
|
11.6
|
1.0
|
CA
|
B:ARG64
|
3.8
|
9.7
|
1.0
|
CB
|
B:THR68
|
4.0
|
10.8
|
1.0
|
CA
|
A:LYS292
|
4.0
|
11.2
|
1.0
|
CG
|
A:LEU296
|
4.1
|
11.5
|
1.0
|
CG
|
B:ARG64
|
4.2
|
12.6
|
1.0
|
CG
|
B:ARG67
|
4.3
|
13.3
|
0.5
|
CB
|
A:LYS292
|
4.4
|
11.7
|
1.0
|
O
|
B:HOH502
|
4.6
|
18.0
|
0.5
|
N
|
A:LEU296
|
4.6
|
10.8
|
1.0
|
N
|
B:THR68
|
4.6
|
10.7
|
1.0
|
OD1
|
A:ASP295
|
4.7
|
15.5
|
1.0
|
CA
|
B:THR68
|
4.8
|
11.5
|
1.0
|
CG2
|
B:THR68
|
4.8
|
12.8
|
1.0
|
N
|
B:VAL65
|
4.8
|
10.1
|
1.0
|
CA
|
A:ASP295
|
4.9
|
11.4
|
1.0
|
CG
|
A:LYS292
|
4.9
|
12.9
|
1.0
|
NE
|
B:ARG64
|
4.9
|
11.7
|
1.0
|
CD1
|
A:LEU296
|
4.9
|
10.9
|
1.0
|
C
|
A:ASP295
|
5.0
|
9.3
|
1.0
|
|
Sodium binding site 2 out
of 3 in 6c5b
Go back to
Sodium Binding Sites List in 6c5b
Sodium binding site 2 out
of 3 in the Crystal Structure Analysis of Laphzm
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Crystal Structure Analysis of Laphzm within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na505
b:34.5
occ:1.00
|
O
|
A:HOH718
|
2.0
|
30.2
|
1.0
|
O
|
B:ALA116
|
2.5
|
16.9
|
1.0
|
O
|
A:GLY108
|
2.8
|
11.0
|
1.0
|
O
|
A:HOH740
|
2.8
|
26.0
|
1.0
|
C
|
B:ALA116
|
3.6
|
14.4
|
1.0
|
O
|
B:HOH631
|
3.9
|
11.9
|
1.0
|
C
|
A:GLY108
|
3.9
|
9.9
|
1.0
|
CA
|
A:GLU109
|
4.1
|
9.6
|
1.0
|
NE2
|
A:GLN27
|
4.2
|
10.6
|
1.0
|
NE
|
A:ARG113
|
4.2
|
19.3
|
0.5
|
CA
|
B:ALA116
|
4.2
|
12.0
|
1.0
|
NH2
|
A:ARG113
|
4.2
|
22.7
|
0.5
|
CE2
|
A:TYR30
|
4.3
|
11.1
|
1.0
|
NH1
|
A:ARG113
|
4.4
|
26.9
|
0.5
|
CB
|
B:ALA116
|
4.4
|
12.0
|
1.0
|
N
|
A:GLU109
|
4.5
|
9.9
|
1.0
|
O
|
B:HOH684
|
4.5
|
20.3
|
1.0
|
OE1
|
A:GLN27
|
4.5
|
10.6
|
1.0
|
CZ
|
A:TYR30
|
4.6
|
11.9
|
1.0
|
OH
|
A:TYR30
|
4.6
|
14.1
|
1.0
|
CZ
|
A:ARG113
|
4.6
|
19.6
|
0.5
|
CG
|
A:GLU109
|
4.7
|
11.4
|
1.0
|
N
|
B:ASP117
|
4.7
|
14.3
|
1.0
|
CD
|
A:GLN27
|
4.8
|
9.8
|
1.0
|
O
|
A:GLU109
|
4.8
|
9.8
|
1.0
|
C
|
A:GLU109
|
4.8
|
9.7
|
1.0
|
CD2
|
A:TYR30
|
4.9
|
10.4
|
1.0
|
CB
|
A:GLU109
|
4.9
|
11.2
|
1.0
|
|
Sodium binding site 3 out
of 3 in 6c5b
Go back to
Sodium Binding Sites List in 6c5b
Sodium binding site 3 out
of 3 in the Crystal Structure Analysis of Laphzm
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 3 of Crystal Structure Analysis of Laphzm within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na506
b:19.0
occ:0.33
|
NH1
|
A:ARG67
|
1.0
|
20.1
|
0.7
|
CZ
|
A:ARG67
|
2.1
|
22.6
|
0.7
|
OD2
|
B:ASP295
|
2.6
|
16.0
|
1.0
|
NH2
|
A:ARG67
|
2.7
|
23.5
|
0.7
|
OG1
|
A:THR68
|
2.7
|
16.1
|
1.0
|
O
|
B:LYS292
|
3.1
|
13.2
|
1.0
|
NE
|
A:ARG67
|
3.2
|
19.8
|
0.7
|
CG
|
B:ASP295
|
3.4
|
14.4
|
1.0
|
O
|
A:ARG64
|
3.4
|
11.9
|
1.0
|
CB
|
B:ASP295
|
3.5
|
14.1
|
1.0
|
CD
|
A:ARG67
|
3.8
|
19.4
|
0.7
|
CB
|
A:ARG64
|
3.9
|
13.2
|
1.0
|
CD2
|
B:LEU296
|
3.9
|
16.1
|
1.0
|
C
|
B:LYS292
|
3.9
|
14.2
|
1.0
|
C
|
A:ARG64
|
4.0
|
11.3
|
1.0
|
CA
|
A:ARG64
|
4.0
|
12.2
|
1.0
|
CA
|
B:LYS292
|
4.0
|
13.2
|
1.0
|
CB
|
A:THR68
|
4.2
|
13.3
|
1.0
|
CG
|
A:ARG64
|
4.3
|
15.3
|
1.0
|
CG
|
A:ARG67
|
4.3
|
16.3
|
0.7
|
CB
|
B:LYS292
|
4.3
|
13.4
|
1.0
|
CG
|
B:LEU296
|
4.4
|
12.8
|
1.0
|
OD1
|
B:ASP295
|
4.5
|
17.1
|
1.0
|
O
|
A:HOH601
|
4.6
|
20.5
|
0.5
|
CA
|
B:ASP295
|
4.7
|
12.8
|
1.0
|
N
|
B:LEU296
|
4.8
|
10.8
|
1.0
|
N
|
A:THR68
|
4.8
|
12.1
|
1.0
|
NE
|
A:ARG64
|
4.8
|
15.0
|
1.0
|
CA
|
A:THR68
|
4.9
|
11.8
|
1.0
|
CG
|
B:LYS292
|
4.9
|
16.3
|
1.0
|
CG2
|
A:THR68
|
4.9
|
13.0
|
1.0
|
C
|
B:ASP295
|
4.9
|
11.6
|
1.0
|
|
Reference:
J.Jiang,
D.Guiza Beltran,
A.Schacht,
S.Wright,
L.Zhang,
L.Du.
Functional and Structural Analysis of Phenazine O-Methyltransferase Laphzm From Lysobacter Antibioticus OH13 and One-Pot Enzymatic Synthesis of the Antibiotic Myxin. Acs Chem. Biol. V. 13 1003 2018.
ISSN: ESSN 1554-8937
PubMed: 29510028
DOI: 10.1021/ACSCHEMBIO.8B00062
Page generated: Tue Oct 8 06:30:31 2024
|