Calcium in PDB 3tmn: The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis
Enzymatic activity of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis
All present enzymatic activity of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis:
3.4.24.27;
Protein crystallography data
The structure of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis, PDB code: 3tmn
was solved by
H.M.Holden,
B.W.Matthews,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
10.00 /
1.70
|
Space group
|
P 61 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
94.100,
94.100,
131.400,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
n/a /
n/a
|
Other elements in 3tmn:
The structure of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis
(pdb code 3tmn). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the
The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis, PDB code: 3tmn:
Jump to Calcium binding site number:
1;
2;
3;
4;
Calcium binding site 1 out
of 4 in 3tmn
Go back to
Calcium Binding Sites List in 3tmn
Calcium binding site 1 out
of 4 in the The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ca319
b:10.8
occ:1.00
|
O
|
E:GLU187
|
2.2
|
8.7
|
1.0
|
OE1
|
E:GLU190
|
2.4
|
10.9
|
1.0
|
OD1
|
E:ASP138
|
2.4
|
13.8
|
1.0
|
OE2
|
E:GLU190
|
2.5
|
11.8
|
1.0
|
OD2
|
E:ASP185
|
2.5
|
9.8
|
1.0
|
O
|
E:HOH346
|
2.6
|
11.7
|
1.0
|
OE1
|
E:GLU177
|
2.6
|
13.1
|
1.0
|
CD
|
E:GLU190
|
2.8
|
10.3
|
1.0
|
OE2
|
E:GLU177
|
2.9
|
11.2
|
1.0
|
CD
|
E:GLU177
|
3.1
|
13.1
|
1.0
|
C
|
E:GLU187
|
3.4
|
11.6
|
1.0
|
CG
|
E:ASP138
|
3.4
|
15.9
|
1.0
|
CG
|
E:ASP185
|
3.5
|
14.6
|
1.0
|
OD1
|
E:ASP185
|
3.7
|
13.4
|
1.0
|
CA
|
E:CA320
|
3.9
|
12.9
|
1.0
|
CB
|
E:ASP138
|
4.1
|
9.2
|
1.0
|
N
|
E:GLU187
|
4.2
|
14.1
|
1.0
|
N
|
E:ILE188
|
4.2
|
9.1
|
1.0
|
CG
|
E:GLU190
|
4.2
|
8.6
|
1.0
|
OD2
|
E:ASP138
|
4.3
|
13.7
|
1.0
|
O
|
E:ASP185
|
4.3
|
13.8
|
1.0
|
CA
|
E:GLU187
|
4.3
|
11.3
|
1.0
|
CA
|
E:ILE188
|
4.4
|
13.2
|
1.0
|
O
|
E:HOH469
|
4.4
|
31.4
|
1.0
|
N
|
E:GLY189
|
4.5
|
18.0
|
1.0
|
CG
|
E:GLU177
|
4.5
|
9.6
|
1.0
|
CB
|
E:GLU187
|
4.5
|
11.0
|
1.0
|
O
|
E:HOH350
|
4.5
|
15.6
|
1.0
|
C
|
E:ASP185
|
4.6
|
14.3
|
1.0
|
CB
|
E:ASP185
|
4.8
|
13.4
|
1.0
|
N
|
E:ASP185
|
4.8
|
12.8
|
1.0
|
C
|
E:ILE188
|
4.9
|
17.3
|
1.0
|
CA
|
E:ASP185
|
5.0
|
9.4
|
1.0
|
CB
|
E:GLU177
|
5.0
|
11.3
|
1.0
|
N
|
E:GLU190
|
5.0
|
10.4
|
1.0
|
|
Calcium binding site 2 out
of 4 in 3tmn
Go back to
Calcium Binding Sites List in 3tmn
Calcium binding site 2 out
of 4 in the The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ca320
b:12.9
occ:1.00
|
O
|
E:HOH475
|
2.0
|
24.2
|
1.0
|
OE2
|
E:GLU177
|
2.3
|
11.2
|
1.0
|
OE2
|
E:GLU190
|
2.3
|
11.8
|
1.0
|
O
|
E:HOH353
|
2.4
|
14.5
|
1.0
|
O
|
E:ASN183
|
2.4
|
17.7
|
1.0
|
OD1
|
E:ASP185
|
2.4
|
13.4
|
1.0
|
CD
|
E:GLU177
|
3.3
|
13.1
|
1.0
|
CG
|
E:ASP185
|
3.3
|
14.6
|
1.0
|
CD
|
E:GLU190
|
3.4
|
10.3
|
1.0
|
C
|
E:ASN183
|
3.6
|
19.7
|
1.0
|
OD2
|
E:ASP185
|
3.7
|
9.8
|
1.0
|
CG
|
E:GLU190
|
3.8
|
8.6
|
1.0
|
OE1
|
E:GLU177
|
3.8
|
13.1
|
1.0
|
CA
|
E:CA319
|
3.9
|
10.8
|
1.0
|
O
|
E:LYS182
|
4.0
|
25.9
|
1.0
|
CB
|
E:ASN183
|
4.1
|
22.2
|
1.0
|
OD2
|
E:ASP191
|
4.1
|
16.2
|
1.0
|
CA
|
E:PRO184
|
4.2
|
16.3
|
1.0
|
C
|
E:PRO184
|
4.3
|
21.4
|
1.0
|
CG
|
E:GLU177
|
4.3
|
9.6
|
1.0
|
N
|
E:ASP185
|
4.3
|
12.8
|
1.0
|
N
|
E:PRO184
|
4.3
|
12.1
|
1.0
|
OE1
|
E:GLU190
|
4.4
|
10.9
|
1.0
|
OD1
|
E:ASP191
|
4.4
|
15.0
|
1.0
|
CB
|
E:ASP185
|
4.5
|
13.4
|
1.0
|
CG
|
E:ASP191
|
4.5
|
18.9
|
1.0
|
CA
|
E:ASN183
|
4.6
|
15.8
|
1.0
|
O
|
E:HOH469
|
4.6
|
31.4
|
1.0
|
O
|
E:PRO184
|
4.8
|
17.3
|
1.0
|
ND2
|
E:ASN183
|
4.8
|
51.3
|
1.0
|
CA
|
E:ASP185
|
5.0
|
9.4
|
1.0
|
|
Calcium binding site 3 out
of 4 in 3tmn
Go back to
Calcium Binding Sites List in 3tmn
Calcium binding site 3 out
of 4 in the The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ca321
b:11.2
occ:1.00
|
O
|
E:HOH482
|
2.2
|
15.6
|
1.0
|
OD1
|
E:ASP57
|
2.2
|
14.1
|
1.0
|
O
|
E:GLN61
|
2.2
|
12.3
|
1.0
|
OD1
|
E:ASP59
|
2.4
|
17.4
|
1.0
|
O
|
E:HOH503
|
2.4
|
14.8
|
1.0
|
O
|
E:HOH419
|
2.5
|
13.6
|
1.0
|
OD2
|
E:ASP57
|
2.6
|
11.5
|
1.0
|
CG
|
E:ASP57
|
2.8
|
13.6
|
1.0
|
CG
|
E:ASP59
|
3.4
|
19.1
|
1.0
|
C
|
E:GLN61
|
3.4
|
15.5
|
1.0
|
OD2
|
E:ASP59
|
3.9
|
16.1
|
1.0
|
N
|
E:GLN61
|
4.0
|
12.7
|
1.0
|
O
|
E:HOH484
|
4.0
|
23.9
|
1.0
|
CA
|
E:GLN61
|
4.2
|
15.8
|
1.0
|
CB
|
E:ASP57
|
4.3
|
5.1
|
1.0
|
N
|
E:ASP59
|
4.4
|
11.8
|
1.0
|
CB
|
E:GLN61
|
4.4
|
13.7
|
1.0
|
N
|
E:PHE62
|
4.5
|
13.1
|
1.0
|
O
|
E:HOH508
|
4.6
|
18.0
|
1.0
|
OD2
|
E:ASP67
|
4.6
|
15.0
|
1.0
|
O
|
E:HOH356
|
4.7
|
11.8
|
1.0
|
CB
|
E:ASP59
|
4.7
|
9.7
|
1.0
|
N
|
E:ASN60
|
4.7
|
8.6
|
1.0
|
CA
|
E:PHE62
|
4.7
|
10.9
|
1.0
|
N
|
E:ALA58
|
4.8
|
9.6
|
1.0
|
CA
|
E:ASP59
|
4.9
|
11.5
|
1.0
|
C
|
E:ASP59
|
4.9
|
14.0
|
1.0
|
|
Calcium binding site 4 out
of 4 in 3tmn
Go back to
Calcium Binding Sites List in 3tmn
Calcium binding site 4 out
of 4 in the The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ca322
b:15.1
occ:1.00
|
O
|
E:HOH480
|
2.1
|
28.9
|
1.0
|
O
|
E:ILE197
|
2.2
|
28.8
|
1.0
|
OD1
|
E:ASP200
|
2.3
|
18.9
|
1.0
|
OG1
|
E:THR194
|
2.4
|
15.8
|
1.0
|
O
|
E:THR194
|
2.4
|
18.7
|
1.0
|
O
|
E:TYR193
|
2.5
|
15.4
|
1.0
|
O
|
E:HOH354
|
2.6
|
13.8
|
1.0
|
C
|
E:THR194
|
3.2
|
18.3
|
1.0
|
CG
|
E:ASP200
|
3.3
|
10.1
|
1.0
|
C
|
E:ILE197
|
3.3
|
26.1
|
1.0
|
C
|
E:TYR193
|
3.4
|
14.8
|
1.0
|
CB
|
E:THR194
|
3.5
|
12.7
|
1.0
|
CA
|
E:THR194
|
3.7
|
15.8
|
1.0
|
OD2
|
E:ASP200
|
3.8
|
14.9
|
1.0
|
N
|
E:THR194
|
3.9
|
14.0
|
1.0
|
CA
|
E:ILE197
|
4.1
|
18.0
|
1.0
|
N
|
E:ILE197
|
4.1
|
31.8
|
1.0
|
N
|
E:PRO195
|
4.2
|
22.1
|
1.0
|
N
|
E:SER198
|
4.4
|
28.4
|
1.0
|
CB
|
E:ILE197
|
4.4
|
31.1
|
1.0
|
O
|
E:ASP200
|
4.4
|
15.6
|
1.0
|
O
|
E:GLU190
|
4.5
|
15.0
|
1.0
|
N
|
E:ASP200
|
4.6
|
17.6
|
1.0
|
CA
|
E:SER198
|
4.6
|
30.3
|
1.0
|
CA
|
E:TYR193
|
4.6
|
10.7
|
1.0
|
CB
|
E:ASP200
|
4.7
|
13.2
|
1.0
|
CA
|
E:PRO195
|
4.7
|
15.1
|
1.0
|
CD2
|
E:TYR193
|
4.8
|
14.5
|
1.0
|
CG2
|
E:THR194
|
4.8
|
13.3
|
1.0
|
C
|
E:ASP200
|
4.8
|
9.5
|
1.0
|
O
|
E:HOH505
|
4.9
|
53.4
|
1.0
|
CB
|
E:TYR193
|
4.9
|
13.2
|
1.0
|
C
|
E:PRO195
|
4.9
|
30.7
|
1.0
|
C
|
E:SER198
|
4.9
|
23.9
|
1.0
|
CA
|
E:ASP200
|
5.0
|
9.4
|
1.0
|
|
Reference:
H.M.Holden,
B.W.Matthews.
The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis. J.Biol.Chem. V. 263 3256 1988.
ISSN: ISSN 0021-9258
PubMed: 3343246
Page generated: Sat Jul 13 19:49:29 2024
|