Calcium in PDB 2d3n: Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose
Enzymatic activity of Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose
All present enzymatic activity of Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose:
3.2.1.98;
Protein crystallography data
The structure of Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose, PDB code: 2d3n
was solved by
R.Kanai,
K.Haga,
T.Akiba,
K.Yamane,
K.Harata,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
6.00 /
1.90
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
47.630,
82.690,
126.970,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
15.5 /
18.4
|
Other elements in 2d3n:
The structure of Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose
(pdb code 2d3n). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the
Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose, PDB code: 2d3n:
Jump to Calcium binding site number:
1;
2;
3;
Calcium binding site 1 out
of 3 in 2d3n
Go back to
Calcium Binding Sites List in 2d3n
Calcium binding site 1 out
of 3 in the Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose
 Mono view
 Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca501
b:14.1
occ:1.00
|
OD1
|
A:ASP188
|
2.3
|
17.4
|
1.0
|
O
|
A:ALA186
|
2.3
|
15.8
|
1.0
|
OD1
|
A:ASP207
|
2.4
|
14.6
|
1.0
|
OD2
|
A:ASP209
|
2.5
|
19.4
|
1.0
|
OD1
|
A:ASP163
|
2.5
|
14.2
|
1.0
|
OD2
|
A:ASP163
|
2.5
|
12.9
|
1.0
|
O
|
A:HOH771
|
2.6
|
15.1
|
1.0
|
CG
|
A:ASP163
|
2.8
|
13.6
|
1.0
|
CG
|
A:ASP207
|
3.2
|
14.1
|
1.0
|
CG
|
A:ASP209
|
3.4
|
20.1
|
1.0
|
CG
|
A:ASP188
|
3.4
|
16.7
|
1.0
|
C
|
A:ALA186
|
3.5
|
15.9
|
1.0
|
OD2
|
A:ASP207
|
3.7
|
14.7
|
1.0
|
CB
|
A:ASP209
|
3.8
|
18.9
|
1.0
|
N
|
A:ASP188
|
3.8
|
14.9
|
1.0
|
C
|
A:TRP187
|
4.0
|
16.2
|
1.0
|
OD2
|
A:ASP188
|
4.0
|
15.6
|
1.0
|
CB
|
A:ASP207
|
4.1
|
13.0
|
1.0
|
CA
|
A:ASP188
|
4.2
|
15.4
|
1.0
|
N
|
A:ALA186
|
4.2
|
17.1
|
1.0
|
CB
|
A:ASP163
|
4.3
|
13.3
|
1.0
|
CA
|
A:ASP207
|
4.3
|
13.3
|
1.0
|
N
|
A:ASP209
|
4.3
|
16.9
|
1.0
|
OD1
|
A:ASP209
|
4.4
|
19.2
|
1.0
|
CB
|
A:ASP188
|
4.4
|
14.8
|
1.0
|
O
|
A:TRP187
|
4.4
|
15.5
|
1.0
|
CA
|
A:TRP187
|
4.4
|
14.2
|
1.0
|
N
|
A:TRP187
|
4.4
|
13.8
|
1.0
|
NA
|
A:NA504
|
4.4
|
15.6
|
1.0
|
CA
|
A:ALA186
|
4.5
|
16.9
|
1.0
|
N
|
A:MET208
|
4.6
|
13.9
|
1.0
|
CA
|
A:ASP209
|
4.7
|
17.6
|
1.0
|
C
|
A:ASP207
|
4.7
|
14.0
|
1.0
|
O
|
A:HOH848
|
4.7
|
22.2
|
1.0
|
OD2
|
A:ASP199
|
4.9
|
15.0
|
1.0
|
O
|
A:HOH856
|
4.9
|
22.0
|
1.0
|
|
Calcium binding site 2 out
of 3 in 2d3n
Go back to
Calcium Binding Sites List in 2d3n
Calcium binding site 2 out
of 3 in the Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose
 Mono view
 Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca502
b:14.3
occ:1.00
|
OD1
|
A:ASN106
|
2.3
|
12.3
|
1.0
|
O
|
A:ASP199
|
2.3
|
12.3
|
1.0
|
OD1
|
A:ASP205
|
2.3
|
12.1
|
1.0
|
OD1
|
A:ASP199
|
2.4
|
15.0
|
1.0
|
O
|
A:HIS240
|
2.4
|
11.9
|
1.0
|
O
|
A:HOH721
|
2.4
|
13.7
|
1.0
|
CG
|
A:ASP205
|
3.1
|
13.7
|
1.0
|
OD2
|
A:ASP205
|
3.2
|
16.7
|
1.0
|
C
|
A:ASP199
|
3.3
|
12.7
|
1.0
|
CG
|
A:ASN106
|
3.4
|
13.4
|
1.0
|
CG
|
A:ASP199
|
3.4
|
14.3
|
1.0
|
C
|
A:HIS240
|
3.5
|
12.3
|
1.0
|
CA
|
A:ASP199
|
3.8
|
13.8
|
1.0
|
O
|
A:HOH738
|
3.9
|
13.9
|
1.0
|
NA
|
A:NA504
|
4.0
|
15.6
|
1.0
|
CB
|
A:HIS240
|
4.0
|
11.4
|
1.0
|
O
|
A:ASN106
|
4.1
|
12.2
|
1.0
|
ND2
|
A:ASN106
|
4.1
|
14.9
|
1.0
|
CB
|
A:ASP199
|
4.2
|
14.5
|
1.0
|
OD2
|
A:ASP199
|
4.3
|
15.0
|
1.0
|
O
|
A:HOH717
|
4.3
|
13.7
|
1.0
|
CA
|
A:HIS240
|
4.3
|
11.7
|
1.0
|
N
|
A:TYR200
|
4.4
|
13.4
|
1.0
|
N
|
A:ILE241
|
4.5
|
12.1
|
1.0
|
CB
|
A:ASP205
|
4.5
|
12.9
|
1.0
|
CB
|
A:ASN106
|
4.6
|
12.5
|
1.0
|
CA
|
A:ILE241
|
4.6
|
12.8
|
1.0
|
O
|
A:ILE206
|
4.6
|
14.1
|
1.0
|
CA
|
A:TYR200
|
4.7
|
12.2
|
1.0
|
CA
|
A:ASN106
|
4.8
|
13.0
|
1.0
|
C
|
A:ASN106
|
4.8
|
13.2
|
1.0
|
CG1
|
A:ILE241
|
4.9
|
12.4
|
1.0
|
|
Calcium binding site 3 out
of 3 in 2d3n
Go back to
Calcium Binding Sites List in 2d3n
Calcium binding site 3 out
of 3 in the Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose
 Mono view
 Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of Crystal Structure of Maltohexaose-Producing Amylase From Bacillus Sp.707 Complexed with Maltohexaose within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca503
b:21.1
occ:1.00
|
O
|
A:TYR307
|
2.3
|
17.3
|
1.0
|
O
|
A:HIS408
|
2.4
|
16.0
|
1.0
|
OD1
|
A:ASN409
|
2.5
|
17.1
|
1.0
|
O
|
A:GLY305
|
2.5
|
17.3
|
1.0
|
OD1
|
A:ASP432
|
2.5
|
14.2
|
1.0
|
OD2
|
A:ASP432
|
2.6
|
14.6
|
1.0
|
O
|
A:HOH804
|
2.7
|
19.6
|
1.0
|
CG
|
A:ASP432
|
2.9
|
16.9
|
1.0
|
C
|
A:HIS408
|
3.4
|
15.8
|
1.0
|
C
|
A:GLY305
|
3.4
|
17.4
|
1.0
|
C
|
A:TYR307
|
3.5
|
16.8
|
1.0
|
CG
|
A:ASN409
|
3.6
|
17.2
|
1.0
|
CA
|
A:ASN409
|
3.7
|
15.5
|
1.0
|
N
|
A:TYR307
|
3.7
|
16.5
|
1.0
|
N
|
A:ASN409
|
4.0
|
15.3
|
1.0
|
C
|
A:ASN306
|
4.1
|
17.9
|
1.0
|
CG
|
A:MET309
|
4.1
|
15.1
|
1.0
|
CB
|
A:ASN409
|
4.2
|
16.2
|
1.0
|
N
|
A:ASN306
|
4.2
|
16.8
|
1.0
|
CA
|
A:TYR307
|
4.2
|
17.0
|
1.0
|
CA
|
A:GLY305
|
4.3
|
15.9
|
1.0
|
CA
|
A:ASN306
|
4.3
|
17.3
|
1.0
|
N
|
A:MET309
|
4.3
|
13.4
|
1.0
|
CB
|
A:ASP432
|
4.4
|
13.6
|
1.0
|
N
|
A:ASP308
|
4.5
|
16.4
|
1.0
|
ND1
|
A:HIS408
|
4.6
|
23.0
|
1.0
|
CA
|
A:HIS408
|
4.6
|
17.4
|
1.0
|
O
|
A:HOH776
|
4.6
|
19.8
|
1.0
|
CA
|
A:ASP308
|
4.6
|
14.7
|
1.0
|
CB
|
A:HIS408
|
4.6
|
18.8
|
1.0
|
ND2
|
A:ASN409
|
4.7
|
17.4
|
1.0
|
O
|
A:HOH714
|
4.7
|
12.9
|
1.0
|
O
|
A:HOH796
|
4.7
|
23.7
|
1.0
|
O
|
A:ASN306
|
4.8
|
17.0
|
1.0
|
CB
|
A:TYR307
|
4.8
|
16.8
|
1.0
|
O
|
A:HOH953
|
4.8
|
29.6
|
1.0
|
CB
|
A:MET309
|
4.9
|
15.7
|
1.0
|
C
|
A:ASN409
|
4.9
|
16.1
|
1.0
|
C
|
A:ASP308
|
5.0
|
13.8
|
1.0
|
|
Reference:
R.Kanai,
K.Haga,
T.Akiba,
K.Yamane,
K.Harata.
Role of TRP140 at Subsite -6 on the Maltohexaose Production of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707 Protein Sci. V. 15 468 2006.
ISSN: ISSN 0961-8368
PubMed: 16452622
DOI: 10.1110/PS.051877006
Page generated: Fri Jul 12 09:40:46 2024
|