Calcium in PDB 1srp: Structural Analysis of Serratia Protease
Enzymatic activity of Structural Analysis of Serratia Protease
All present enzymatic activity of Structural Analysis of Serratia Protease:
3.4.24.40;
Protein crystallography data
The structure of Structural Analysis of Serratia Protease, PDB code: 1srp
was solved by
K.Hamada,
H.Hiramatsu,
Y.Katsuya,
Y.Hata,
Y.Katsube,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
8.00 /
2.00
|
|
Space group
|
P 21 21 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
109.140,
150.890,
42.640,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
n/a /
n/a
|
Other elements in 1srp:
The structure of Structural Analysis of Serratia Protease also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structural Analysis of Serratia Protease
(pdb code 1srp). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 7 binding sites of Calcium where determined in the
Structural Analysis of Serratia Protease, PDB code: 1srp:
Jump to Calcium binding site number:
1;
2;
3;
4;
5;
6;
7;
Calcium binding site 1 out
of 7 in 1srp
Go back to
Calcium Binding Sites List in 1srp
Calcium binding site 1 out
of 7 in the Structural Analysis of Serratia Protease
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Structural Analysis of Serratia Protease within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca911
b:20.4
occ:1.00
|
O
|
A:ARG253
|
2.3
|
15.4
|
1.0
|
|
OD1
|
A:ASP290
|
2.3
|
13.7
|
1.0
|
|
O
|
A:GLY287
|
2.4
|
15.0
|
1.0
|
|
O
|
A:GLY255
|
2.5
|
13.9
|
1.0
|
|
OD1
|
A:ASP285
|
2.5
|
11.8
|
1.0
|
|
OG1
|
A:THR257
|
2.5
|
13.2
|
1.0
|
|
OD2
|
A:ASP285
|
2.6
|
10.4
|
1.0
|
|
CG
|
A:ASP285
|
2.9
|
11.4
|
1.0
|
|
CG
|
A:ASP290
|
3.2
|
12.8
|
1.0
|
|
OD2
|
A:ASP290
|
3.3
|
12.2
|
1.0
|
|
C
|
A:ARG253
|
3.4
|
14.2
|
1.0
|
|
C
|
A:GLY287
|
3.6
|
14.6
|
1.0
|
|
CB
|
A:THR257
|
3.6
|
13.0
|
1.0
|
|
C
|
A:GLY255
|
3.7
|
14.4
|
1.0
|
|
N
|
A:THR257
|
3.8
|
13.4
|
1.0
|
|
C
|
A:THR254
|
4.1
|
14.7
|
1.0
|
|
N
|
A:GLY255
|
4.1
|
14.5
|
1.0
|
|
CB
|
A:ARG253
|
4.1
|
13.0
|
1.0
|
|
N
|
A:GLY287
|
4.2
|
14.1
|
1.0
|
|
CA
|
A:THR254
|
4.3
|
14.3
|
1.0
|
|
CA
|
A:GLY288
|
4.3
|
14.6
|
1.0
|
|
N
|
A:THR254
|
4.3
|
14.5
|
1.0
|
|
CA
|
A:ARG253
|
4.4
|
14.0
|
1.0
|
|
CA
|
A:THR257
|
4.4
|
13.2
|
1.0
|
|
CB
|
A:ASP285
|
4.4
|
11.4
|
1.0
|
|
N
|
A:GLY288
|
4.4
|
14.9
|
1.0
|
|
O
|
A:HOH601
|
4.4
|
17.7
|
1.0
|
|
O
|
A:HOH550
|
4.5
|
15.2
|
1.0
|
|
O
|
A:THR254
|
4.5
|
14.5
|
1.0
|
|
CB
|
A:ASP290
|
4.5
|
12.9
|
1.0
|
|
C
|
A:ASP256
|
4.5
|
13.8
|
1.0
|
|
N
|
A:ASP256
|
4.5
|
14.3
|
1.0
|
|
CA
|
A:GLY255
|
4.6
|
14.6
|
1.0
|
|
CA
|
A:GLY287
|
4.6
|
14.7
|
1.0
|
|
CA
|
A:ASP256
|
4.6
|
14.3
|
1.0
|
|
C
|
A:GLY288
|
4.7
|
14.6
|
1.0
|
|
CG2
|
A:THR257
|
4.8
|
11.8
|
1.0
|
|
O
|
A:GLY288
|
4.9
|
13.1
|
1.0
|
|
Calcium binding site 2 out
of 7 in 1srp
Go back to
Calcium Binding Sites List in 1srp
Calcium binding site 2 out
of 7 in the Structural Analysis of Serratia Protease
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of Structural Analysis of Serratia Protease within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca912
b:21.1
occ:1.00
|
OD2
|
A:ASP290
|
2.5
|
12.2
|
1.0
|
|
O
|
A:GLY288
|
2.5
|
13.1
|
1.0
|
|
O
|
A:THR327
|
2.5
|
11.7
|
1.0
|
|
OE1
|
A:GLU329
|
2.5
|
12.7
|
1.0
|
|
O
|
A:HOH550
|
2.6
|
15.2
|
1.0
|
|
O
|
A:HOH524
|
2.7
|
13.8
|
1.0
|
|
OE2
|
A:GLU329
|
2.7
|
14.0
|
1.0
|
|
CD
|
A:GLU329
|
3.0
|
12.9
|
1.0
|
|
CG
|
A:ASP290
|
3.6
|
12.8
|
1.0
|
|
C
|
A:GLY288
|
3.6
|
14.6
|
1.0
|
|
C
|
A:THR327
|
3.7
|
11.4
|
1.0
|
|
N
|
A:ASP290
|
4.2
|
14.2
|
1.0
|
|
N
|
A:GLY288
|
4.2
|
14.9
|
1.0
|
|
C
|
A:GLY287
|
4.2
|
14.6
|
1.0
|
|
O
|
A:GLY287
|
4.3
|
15.0
|
1.0
|
|
OD1
|
A:ASP290
|
4.3
|
13.7
|
1.0
|
|
CB
|
A:ASP290
|
4.3
|
12.9
|
1.0
|
|
CA
|
A:GLY288
|
4.4
|
14.6
|
1.0
|
|
CB
|
A:THR327
|
4.5
|
11.1
|
1.0
|
|
N
|
A:ASN289
|
4.5
|
15.1
|
1.0
|
|
OD1
|
A:ASP285
|
4.5
|
11.8
|
1.0
|
|
O
|
A:HOH526
|
4.5
|
13.0
|
1.0
|
|
CA
|
A:ASN289
|
4.5
|
15.6
|
1.0
|
|
CG
|
A:GLU329
|
4.5
|
11.8
|
1.0
|
|
CA
|
A:THR327
|
4.6
|
11.8
|
1.0
|
|
N
|
A:ILE328
|
4.6
|
11.7
|
1.0
|
|
O
|
A:HOH607
|
4.6
|
22.0
|
1.0
|
|
CA
|
A:ILE328
|
4.6
|
11.2
|
1.0
|
|
C
|
A:ASN289
|
4.8
|
14.8
|
1.0
|
|
CA
|
A:GLY287
|
4.8
|
14.7
|
1.0
|
|
N
|
A:THR327
|
4.8
|
11.8
|
1.0
|
|
N
|
A:GLU329
|
4.8
|
10.9
|
1.0
|
|
CG2
|
A:THR327
|
4.9
|
10.3
|
1.0
|
|
CA
|
A:ASP290
|
4.9
|
13.9
|
1.0
|
|
Calcium binding site 3 out
of 7 in 1srp
Go back to
Calcium Binding Sites List in 1srp
Calcium binding site 3 out
of 7 in the Structural Analysis of Serratia Protease
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of Structural Analysis of Serratia Protease within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca913
b:21.4
occ:1.00
|
O
|
A:GLY334
|
2.3
|
13.9
|
1.0
|
|
OD1
|
A:ASP356
|
2.4
|
13.1
|
1.0
|
|
O
|
A:ALA353
|
2.4
|
16.5
|
1.0
|
|
O
|
A:GLY351
|
2.5
|
15.9
|
1.0
|
|
O
|
A:GLY336
|
2.5
|
14.5
|
1.0
|
|
OD2
|
A:ASP338
|
2.6
|
14.9
|
1.0
|
|
OD2
|
A:ASP356
|
2.9
|
12.9
|
1.0
|
|
CG
|
A:ASP356
|
3.0
|
13.2
|
1.0
|
|
CG
|
A:ASP338
|
3.4
|
14.2
|
1.0
|
|
C
|
A:GLY334
|
3.5
|
14.3
|
1.0
|
|
C
|
A:GLY351
|
3.5
|
16.2
|
1.0
|
|
C
|
A:ALA353
|
3.6
|
16.7
|
1.0
|
|
C
|
A:GLY336
|
3.7
|
14.8
|
1.0
|
|
C
|
A:GLY352
|
3.9
|
16.6
|
1.0
|
|
O
|
A:GLY352
|
4.0
|
17.2
|
1.0
|
|
N
|
A:GLY336
|
4.0
|
15.2
|
1.0
|
|
OD1
|
A:ASP338
|
4.1
|
14.4
|
1.0
|
|
N
|
A:GLY334
|
4.1
|
14.3
|
1.0
|
|
CB
|
A:ASP338
|
4.1
|
13.8
|
1.0
|
|
N
|
A:ALA353
|
4.2
|
16.4
|
1.0
|
|
N
|
A:ASP338
|
4.2
|
13.3
|
1.0
|
|
C
|
A:SER335
|
4.2
|
16.0
|
1.0
|
|
CA
|
A:GLY352
|
4.3
|
16.9
|
1.0
|
|
N
|
A:GLY352
|
4.3
|
16.3
|
1.0
|
|
CA
|
A:GLY354
|
4.3
|
15.6
|
1.0
|
|
N
|
A:SER335
|
4.4
|
15.4
|
1.0
|
|
CA
|
A:SER335
|
4.4
|
16.2
|
1.0
|
|
CA
|
A:GLY351
|
4.4
|
15.7
|
1.0
|
|
N
|
A:GLY354
|
4.4
|
16.4
|
1.0
|
|
O
|
A:HOH501
|
4.4
|
8.5
|
1.0
|
|
CB
|
A:ASP356
|
4.5
|
13.5
|
1.0
|
|
CA
|
A:GLY334
|
4.5
|
14.4
|
1.0
|
|
CA
|
A:GLY336
|
4.5
|
14.5
|
1.0
|
|
CA
|
A:ALA353
|
4.6
|
16.5
|
1.0
|
|
C
|
A:GLY333
|
4.6
|
14.2
|
1.0
|
|
N
|
A:ASN337
|
4.6
|
14.1
|
1.0
|
|
C
|
A:GLY354
|
4.6
|
15.2
|
1.0
|
|
O
|
A:GLY354
|
4.7
|
15.7
|
1.0
|
|
CA
|
A:CA915
|
4.7
|
19.6
|
1.0
|
|
CA
|
A:ASN337
|
4.8
|
14.2
|
1.0
|
|
O
|
A:SER335
|
4.8
|
15.7
|
1.0
|
|
CA
|
A:GLY333
|
4.8
|
14.2
|
1.0
|
|
CA
|
A:ASP338
|
4.9
|
13.4
|
1.0
|
|
C
|
A:ASN337
|
4.9
|
13.9
|
1.0
|
|
Calcium binding site 4 out
of 7 in 1srp
Go back to
Calcium Binding Sites List in 1srp
Calcium binding site 4 out
of 7 in the Structural Analysis of Serratia Protease
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of Structural Analysis of Serratia Protease within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca914
b:18.9
occ:1.00
|
O
|
A:GLY362
|
2.4
|
10.2
|
1.0
|
|
O
|
A:ASN343
|
2.4
|
10.9
|
1.0
|
|
O
|
A:GLY360
|
2.5
|
13.5
|
1.0
|
|
O
|
A:ALA345
|
2.5
|
12.4
|
1.0
|
|
OD1
|
A:ASN347
|
2.5
|
9.6
|
1.0
|
|
OD1
|
A:ASP365
|
2.6
|
9.7
|
1.0
|
|
OD2
|
A:ASP365
|
2.9
|
8.7
|
1.0
|
|
CG
|
A:ASP365
|
3.1
|
8.8
|
1.0
|
|
CG
|
A:ASN347
|
3.4
|
8.8
|
1.0
|
|
C
|
A:GLY360
|
3.5
|
13.0
|
1.0
|
|
C
|
A:GLY362
|
3.6
|
11.3
|
1.0
|
|
C
|
A:ASN343
|
3.6
|
11.6
|
1.0
|
|
C
|
A:ALA345
|
3.7
|
12.6
|
1.0
|
|
C
|
A:GLY361
|
3.9
|
12.7
|
1.0
|
|
N
|
A:GLY362
|
4.0
|
12.1
|
1.0
|
|
N
|
A:ASN343
|
4.1
|
11.1
|
1.0
|
|
O
|
A:GLY361
|
4.1
|
13.4
|
1.0
|
|
N
|
A:ALA345
|
4.1
|
11.8
|
1.0
|
|
ND2
|
A:ASN347
|
4.1
|
8.6
|
1.0
|
|
C
|
A:ALA344
|
4.2
|
11.6
|
1.0
|
|
N
|
A:ASN347
|
4.2
|
10.5
|
1.0
|
|
CB
|
A:ASN347
|
4.2
|
9.7
|
1.0
|
|
CA
|
A:GLY361
|
4.3
|
12.8
|
1.0
|
|
N
|
A:GLY361
|
4.3
|
12.4
|
1.0
|
|
CA
|
A:GLY362
|
4.4
|
11.7
|
1.0
|
|
CA
|
A:GLY360
|
4.4
|
13.1
|
1.0
|
|
CA
|
A:CA916
|
4.4
|
24.4
|
1.0
|
|
CA
|
A:ALA344
|
4.4
|
11.5
|
1.0
|
|
N
|
A:ALA344
|
4.4
|
11.3
|
1.0
|
|
ND2
|
A:ASN343
|
4.5
|
11.0
|
1.0
|
|
CA
|
A:ASN343
|
4.5
|
10.9
|
1.0
|
|
N
|
A:GLY363
|
4.5
|
11.9
|
1.0
|
|
CA
|
A:GLY363
|
4.6
|
11.8
|
1.0
|
|
CB
|
A:ASP365
|
4.6
|
10.1
|
1.0
|
|
CA
|
A:ALA345
|
4.6
|
12.1
|
1.0
|
|
CA
|
A:ASN346
|
4.6
|
11.1
|
1.0
|
|
O
|
A:ALA344
|
4.7
|
11.8
|
1.0
|
|
C
|
A:ASN346
|
4.7
|
10.8
|
1.0
|
|
N
|
A:ASN346
|
4.7
|
11.2
|
1.0
|
|
C
|
A:GLY342
|
4.7
|
11.1
|
1.0
|
|
CA
|
A:ASN347
|
4.9
|
10.2
|
1.0
|
|
C
|
A:GLY363
|
4.9
|
11.8
|
1.0
|
|
CA
|
A:GLY342
|
4.9
|
11.0
|
1.0
|
|
O
|
A:GLY363
|
5.0
|
12.1
|
1.0
|
|
Calcium binding site 5 out
of 7 in 1srp
Go back to
Calcium Binding Sites List in 1srp
Calcium binding site 5 out
of 7 in the Structural Analysis of Serratia Protease
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 5 of Structural Analysis of Serratia Protease within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca915
b:19.6
occ:1.00
|
O
|
A:ALA371
|
2.3
|
16.4
|
1.0
|
|
O
|
A:GLY352
|
2.4
|
17.2
|
1.0
|
|
OD2
|
A:ASP356
|
2.4
|
12.9
|
1.0
|
|
O
|
A:GLY369
|
2.5
|
14.2
|
1.0
|
|
OD1
|
A:ASP374
|
2.6
|
17.2
|
1.0
|
|
O
|
A:GLY354
|
2.6
|
15.7
|
1.0
|
|
OD2
|
A:ASP374
|
2.9
|
17.1
|
1.0
|
|
CG
|
A:ASP374
|
3.1
|
16.4
|
1.0
|
|
CG
|
A:ASP356
|
3.5
|
13.2
|
1.0
|
|
C
|
A:ALA371
|
3.5
|
16.8
|
1.0
|
|
C
|
A:GLY369
|
3.6
|
13.5
|
1.0
|
|
C
|
A:GLY352
|
3.6
|
16.6
|
1.0
|
|
C
|
A:GLY354
|
3.8
|
15.2
|
1.0
|
|
C
|
A:ALA353
|
3.8
|
16.7
|
1.0
|
|
N
|
A:ALA371
|
3.9
|
16.0
|
1.0
|
|
O
|
A:ALA353
|
3.9
|
16.5
|
1.0
|
|
C
|
A:GLY370
|
4.0
|
15.6
|
1.0
|
|
CB
|
A:ASP356
|
4.1
|
13.5
|
1.0
|
|
N
|
A:GLY354
|
4.1
|
16.4
|
1.0
|
|
N
|
A:ASP356
|
4.2
|
13.6
|
1.0
|
|
CA
|
A:ALA353
|
4.2
|
16.5
|
1.0
|
|
CA
|
A:GLY370
|
4.3
|
14.6
|
1.0
|
|
N
|
A:GLY352
|
4.3
|
16.3
|
1.0
|
|
C
|
A:GLY351
|
4.3
|
16.2
|
1.0
|
|
N
|
A:GLY370
|
4.3
|
14.2
|
1.0
|
|
OD1
|
A:ASP356
|
4.4
|
13.1
|
1.0
|
|
N
|
A:ALA353
|
4.4
|
16.4
|
1.0
|
|
CA
|
A:ALA371
|
4.4
|
16.5
|
1.0
|
|
N
|
A:GLY372
|
4.4
|
17.1
|
1.0
|
|
O
|
A:GLY370
|
4.4
|
16.3
|
1.0
|
|
CA
|
A:GLY369
|
4.4
|
13.3
|
1.0
|
|
CA
|
A:GLY372
|
4.5
|
17.0
|
1.0
|
|
CA
|
A:GLY354
|
4.5
|
15.6
|
1.0
|
|
CB
|
A:ASP374
|
4.6
|
15.2
|
1.0
|
|
CA
|
A:GLY351
|
4.6
|
15.7
|
1.0
|
|
N
|
A:ASN355
|
4.7
|
14.4
|
1.0
|
|
CA
|
A:GLY352
|
4.7
|
16.9
|
1.0
|
|
O
|
A:GLY351
|
4.7
|
15.9
|
1.0
|
|
CA
|
A:CA913
|
4.7
|
21.4
|
1.0
|
|
CA
|
A:ASN355
|
4.8
|
14.2
|
1.0
|
|
C
|
A:GLY372
|
4.8
|
16.6
|
1.0
|
|
CA
|
A:ASP356
|
4.9
|
13.5
|
1.0
|
|
C
|
A:ASN355
|
5.0
|
13.8
|
1.0
|
|
Calcium binding site 6 out
of 7 in 1srp
Go back to
Calcium Binding Sites List in 1srp
Calcium binding site 6 out
of 7 in the Structural Analysis of Serratia Protease
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 6 of Structural Analysis of Serratia Protease within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca916
b:24.4
occ:1.00
|
OD2
|
A:ASP365
|
2.2
|
8.7
|
1.0
|
|
O
|
A:ASP383
|
2.2
|
12.2
|
1.0
|
|
O
|
A:GLY361
|
2.5
|
13.4
|
1.0
|
|
O
|
A:GLY363
|
2.5
|
12.1
|
1.0
|
|
OD1
|
A:ASP390
|
2.5
|
13.6
|
1.0
|
|
O
|
A:HOH604
|
2.7
|
14.7
|
1.0
|
|
CG
|
A:ASP365
|
3.2
|
8.8
|
1.0
|
|
CG
|
A:ASP390
|
3.3
|
14.3
|
1.0
|
|
OD2
|
A:ASP390
|
3.4
|
15.6
|
1.0
|
|
O
|
A:GLY362
|
3.4
|
10.2
|
1.0
|
|
C
|
A:ASP383
|
3.4
|
12.7
|
1.0
|
|
C
|
A:GLY363
|
3.5
|
11.8
|
1.0
|
|
C
|
A:GLY362
|
3.6
|
11.3
|
1.0
|
|
C
|
A:GLY361
|
3.6
|
12.7
|
1.0
|
|
CB
|
A:ASP365
|
4.0
|
10.1
|
1.0
|
|
CA
|
A:ASP383
|
4.0
|
12.9
|
1.0
|
|
N
|
A:GLY363
|
4.0
|
11.9
|
1.0
|
|
OD1
|
A:ASP365
|
4.1
|
9.7
|
1.0
|
|
N
|
A:ASP365
|
4.1
|
11.1
|
1.0
|
|
CA
|
A:GLY362
|
4.1
|
11.7
|
1.0
|
|
C
|
A:GLY360
|
4.2
|
13.0
|
1.0
|
|
N
|
A:GLY361
|
4.3
|
12.4
|
1.0
|
|
N
|
A:GLY362
|
4.3
|
12.1
|
1.0
|
|
CA
|
A:GLY363
|
4.3
|
11.8
|
1.0
|
|
N
|
A:ALA364
|
4.4
|
11.5
|
1.0
|
|
CA
|
A:CA914
|
4.4
|
18.9
|
1.0
|
|
O
|
A:GLY360
|
4.5
|
13.5
|
1.0
|
|
N
|
A:SER384
|
4.5
|
12.5
|
1.0
|
|
CA
|
A:GLY360
|
4.5
|
13.1
|
1.0
|
|
O
|
A:HOH516
|
4.6
|
18.3
|
1.0
|
|
CB
|
A:ASP383
|
4.6
|
12.7
|
1.0
|
|
CA
|
A:ALA364
|
4.6
|
11.3
|
1.0
|
|
CA
|
A:GLY361
|
4.6
|
12.8
|
1.0
|
|
CB
|
A:ASP390
|
4.7
|
14.6
|
1.0
|
|
CA
|
A:SER384
|
4.7
|
13.6
|
1.0
|
|
CA
|
A:ASP365
|
4.8
|
11.2
|
1.0
|
|
C
|
A:ALA364
|
4.8
|
11.3
|
1.0
|
|
Calcium binding site 7 out
of 7 in 1srp
Go back to
Calcium Binding Sites List in 1srp
Calcium binding site 7 out
of 7 in the Structural Analysis of Serratia Protease
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 7 of Structural Analysis of Serratia Protease within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca917
b:24.6
occ:1.00
|
OD2
|
A:ASP374
|
2.5
|
17.1
|
1.0
|
|
OD1
|
A:ASP400
|
2.6
|
11.7
|
1.0
|
|
O
|
A:GLY372
|
2.6
|
16.9
|
1.0
|
|
OD2
|
A:ASP400
|
3.2
|
11.2
|
1.0
|
|
O
|
A:HOH527
|
3.2
|
16.7
|
1.0
|
|
O
|
A:GLY370
|
3.2
|
16.3
|
1.0
|
|
CG
|
A:ASP400
|
3.2
|
12.2
|
1.0
|
|
CG
|
A:ASP374
|
3.5
|
16.4
|
1.0
|
|
O
|
A:HOH591
|
3.6
|
19.3
|
1.0
|
|
C
|
A:GLY372
|
3.6
|
16.6
|
1.0
|
|
N
|
A:ASP374
|
4.0
|
14.8
|
1.0
|
|
CB
|
A:ASP374
|
4.0
|
15.2
|
1.0
|
|
C
|
A:ALA371
|
4.1
|
16.8
|
1.0
|
|
O
|
A:ALA371
|
4.1
|
16.4
|
1.0
|
|
N
|
A:GLY372
|
4.2
|
17.1
|
1.0
|
|
C
|
A:GLY370
|
4.3
|
15.6
|
1.0
|
|
N
|
A:LYS373
|
4.4
|
16.3
|
1.0
|
|
CA
|
A:GLY372
|
4.5
|
17.0
|
1.0
|
|
CG
|
A:GLN396
|
4.5
|
22.3
|
1.0
|
|
NE2
|
A:GLN396
|
4.5
|
26.7
|
1.0
|
|
CA
|
A:LYS373
|
4.5
|
16.7
|
1.0
|
|
CA
|
A:ALA371
|
4.5
|
16.5
|
1.0
|
|
OD1
|
A:ASP374
|
4.6
|
17.2
|
1.0
|
|
CG2
|
A:ILE399
|
4.6
|
14.3
|
1.0
|
|
C
|
A:LYS373
|
4.6
|
15.7
|
1.0
|
|
CB
|
A:ASP400
|
4.7
|
11.8
|
1.0
|
|
CA
|
A:ASP374
|
4.7
|
14.5
|
1.0
|
|
C
|
A:GLY369
|
4.7
|
13.5
|
1.0
|
|
N
|
A:ALA371
|
4.8
|
16.0
|
1.0
|
|
N
|
A:GLY370
|
4.8
|
14.2
|
1.0
|
|
CA
|
A:GLY369
|
4.9
|
13.3
|
1.0
|
|
CB
|
A:GLN396
|
4.9
|
18.2
|
1.0
|
|
O
|
A:ASP394
|
5.0
|
14.6
|
1.0
|
|
O
|
A:GLY369
|
5.0
|
14.2
|
1.0
|
|
Reference:
K.Hamada,
Y.Hata,
Y.Katsuya,
H.Hiramatsu,
T.Fujiwara,
Y.Katsube.
Crystal Structure of Serratia Protease, A Zinc-Dependent Proteinase From Serratia Sp. E-15, Containing A Beta-Sheet Coil Motif at 2.0 A Resolution. J.Biochem.(Tokyo) V. 119 844 1996.
ISSN: ISSN 0021-924X
PubMed: 8797082
Page generated: Sat Dec 12 03:20:02 2020
|
