Zinc in PDB 3fvl: Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group
Enzymatic activity of Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group
All present enzymatic activity of Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group:
3.4.17.1;
Protein crystallography data
The structure of Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group, PDB code: 3fvl
was solved by
S.F.Wang,
J.-Y.Jin,
G.R.Tian,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
1.85
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
73.347,
59.786,
99.360,
90.00,
103.94,
90.00
|
R / Rfree (%)
|
20.9 /
23.8
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group
(pdb code 3fvl). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group, PDB code: 3fvl:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 3fvl
Go back to
Zinc Binding Sites List in 3fvl
Zinc binding site 1 out
of 3 in the Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1309
b:12.0
occ:1.00
|
ND1
|
A:HIS69
|
2.1
|
8.2
|
1.0
|
ND1
|
A:HIS196
|
2.1
|
7.4
|
1.0
|
OE1
|
A:GLU72
|
2.2
|
9.7
|
1.0
|
OAO
|
A:BHK311
|
2.3
|
30.6
|
1.0
|
OE2
|
A:GLU72
|
2.3
|
8.4
|
1.0
|
CD
|
A:GLU72
|
2.6
|
10.6
|
1.0
|
CE1
|
A:HIS69
|
3.0
|
8.7
|
1.0
|
CG
|
A:HIS196
|
3.0
|
7.2
|
1.0
|
CG
|
A:HIS69
|
3.1
|
5.8
|
1.0
|
CE1
|
A:HIS196
|
3.1
|
10.2
|
1.0
|
CB
|
A:HIS196
|
3.3
|
6.5
|
1.0
|
CAE
|
A:BHK311
|
3.4
|
36.6
|
1.0
|
CB
|
A:HIS69
|
3.4
|
8.7
|
1.0
|
OAP
|
A:BHK311
|
4.0
|
28.0
|
1.0
|
O
|
A:HOH310
|
4.0
|
9.1
|
1.0
|
CAF
|
A:BHK311
|
4.1
|
34.8
|
1.0
|
CG
|
A:GLU72
|
4.1
|
8.4
|
1.0
|
CA
|
A:HIS196
|
4.1
|
8.2
|
1.0
|
NE2
|
A:HIS69
|
4.1
|
6.8
|
1.0
|
OE2
|
A:GLU270
|
4.2
|
10.7
|
1.0
|
CD2
|
A:HIS196
|
4.2
|
9.9
|
1.0
|
CD2
|
A:HIS69
|
4.2
|
5.6
|
1.0
|
NE2
|
A:HIS196
|
4.2
|
8.7
|
1.0
|
N
|
A:SER197
|
4.4
|
9.1
|
1.0
|
O
|
A:HOH335
|
4.5
|
11.8
|
1.0
|
NH2
|
A:ARG127
|
4.5
|
14.2
|
1.0
|
CAA
|
A:BHK311
|
4.5
|
38.9
|
1.0
|
OAN
|
A:BHK311
|
4.6
|
45.8
|
1.0
|
OE1
|
A:GLU270
|
4.7
|
13.5
|
1.0
|
CAB
|
A:BHK311
|
4.7
|
42.0
|
1.0
|
CA
|
A:HIS69
|
4.8
|
8.9
|
1.0
|
C
|
A:HIS196
|
4.8
|
7.7
|
1.0
|
CD
|
A:GLU270
|
4.9
|
12.9
|
1.0
|
CG2
|
A:ILE68
|
4.9
|
12.2
|
1.0
|
N
|
A:HIS69
|
4.9
|
7.7
|
1.0
|
CB
|
A:GLU72
|
4.9
|
7.8
|
1.0
|
|
Zinc binding site 2 out
of 3 in 3fvl
Go back to
Zinc Binding Sites List in 3fvl
Zinc binding site 2 out
of 3 in the Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn1309
b:15.1
occ:1.00
|
ND1
|
C:HIS69
|
2.2
|
11.1
|
1.0
|
ND1
|
C:HIS196
|
2.2
|
10.7
|
1.0
|
OE1
|
C:GLU72
|
2.2
|
12.8
|
1.0
|
OAO
|
C:BHK311
|
2.2
|
28.5
|
1.0
|
OE2
|
C:GLU72
|
2.4
|
11.3
|
1.0
|
CD
|
C:GLU72
|
2.6
|
12.3
|
1.0
|
CG
|
C:HIS196
|
3.0
|
10.1
|
1.0
|
CG
|
C:HIS69
|
3.1
|
10.7
|
1.0
|
CE1
|
C:HIS69
|
3.1
|
13.2
|
1.0
|
CB
|
C:HIS196
|
3.2
|
10.6
|
1.0
|
CE1
|
C:HIS196
|
3.2
|
13.0
|
1.0
|
CAE
|
C:BHK311
|
3.4
|
35.3
|
1.0
|
CB
|
C:HIS69
|
3.4
|
9.7
|
1.0
|
O
|
C:HOH338
|
3.9
|
11.7
|
1.0
|
CA
|
C:HIS196
|
4.1
|
9.4
|
1.0
|
OAP
|
C:BHK311
|
4.1
|
29.6
|
1.0
|
CG
|
C:GLU72
|
4.1
|
10.8
|
1.0
|
CAF
|
C:BHK311
|
4.2
|
33.2
|
1.0
|
OE2
|
C:GLU270
|
4.2
|
17.3
|
1.0
|
CD2
|
C:HIS196
|
4.2
|
11.3
|
1.0
|
NE2
|
C:HIS69
|
4.3
|
11.9
|
1.0
|
CD2
|
C:HIS69
|
4.3
|
10.0
|
1.0
|
NE2
|
C:HIS196
|
4.3
|
12.6
|
1.0
|
OAN
|
C:BHK311
|
4.4
|
43.6
|
1.0
|
N
|
C:SER197
|
4.4
|
11.5
|
1.0
|
NH2
|
C:ARG127
|
4.5
|
17.1
|
1.0
|
O
|
C:HOH322
|
4.5
|
15.2
|
1.0
|
CAA
|
C:BHK311
|
4.5
|
38.4
|
1.0
|
CAB
|
C:BHK311
|
4.6
|
41.1
|
1.0
|
OE1
|
C:GLU270
|
4.7
|
17.4
|
1.0
|
CA
|
C:HIS69
|
4.8
|
10.4
|
1.0
|
C
|
C:HIS196
|
4.8
|
11.2
|
1.0
|
CG2
|
C:ILE68
|
4.9
|
12.2
|
1.0
|
CD
|
C:GLU270
|
4.9
|
15.4
|
1.0
|
CAC
|
C:BHK311
|
4.9
|
42.2
|
1.0
|
N
|
C:HIS69
|
4.9
|
9.7
|
1.0
|
CB
|
C:GLU72
|
5.0
|
9.3
|
1.0
|
|
Zinc binding site 3 out
of 3 in 3fvl
Go back to
Zinc Binding Sites List in 3fvl
Zinc binding site 3 out
of 3 in the Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystallogic Studies on the Complex of Carboxypeptidase A with Inhibitors Using Alpha-Hydroxy Ketone As Zinc-Binding Group within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn1309
b:13.9
occ:1.00
|
ND1
|
E:HIS69
|
2.1
|
8.4
|
1.0
|
ND1
|
E:HIS196
|
2.2
|
11.2
|
1.0
|
OE1
|
E:GLU72
|
2.3
|
11.1
|
1.0
|
OAO
|
E:BHK311
|
2.3
|
44.0
|
1.0
|
OE2
|
E:GLU72
|
2.3
|
10.8
|
1.0
|
CD
|
E:GLU72
|
2.6
|
11.8
|
1.0
|
CG
|
E:HIS196
|
3.1
|
12.0
|
1.0
|
CG
|
E:HIS69
|
3.1
|
7.0
|
1.0
|
CE1
|
E:HIS69
|
3.1
|
11.4
|
1.0
|
CE1
|
E:HIS196
|
3.2
|
15.7
|
1.0
|
CB
|
E:HIS196
|
3.3
|
10.8
|
1.0
|
CB
|
E:HIS69
|
3.4
|
7.7
|
1.0
|
CAE
|
E:BHK311
|
3.4
|
47.6
|
1.0
|
OAP
|
E:BHK311
|
3.9
|
39.8
|
1.0
|
O
|
E:HOH312
|
4.0
|
9.9
|
1.0
|
CAF
|
E:BHK311
|
4.0
|
45.8
|
1.0
|
CG
|
E:GLU72
|
4.1
|
10.1
|
1.0
|
CA
|
E:HIS196
|
4.2
|
10.8
|
1.0
|
CD2
|
E:HIS196
|
4.2
|
13.5
|
1.0
|
CD2
|
E:HIS69
|
4.2
|
9.3
|
1.0
|
NE2
|
E:HIS69
|
4.2
|
9.2
|
1.0
|
OE2
|
E:GLU270
|
4.3
|
15.9
|
1.0
|
NE2
|
E:HIS196
|
4.3
|
12.5
|
1.0
|
O
|
E:HOH320
|
4.3
|
12.1
|
1.0
|
N
|
E:SER197
|
4.5
|
11.7
|
1.0
|
OAN
|
E:BHK311
|
4.5
|
56.7
|
1.0
|
CAA
|
E:BHK311
|
4.6
|
51.0
|
1.0
|
NH2
|
E:ARG127
|
4.6
|
16.5
|
1.0
|
OE1
|
E:GLU270
|
4.7
|
15.3
|
1.0
|
CA
|
E:HIS69
|
4.7
|
9.1
|
1.0
|
CAB
|
E:BHK311
|
4.8
|
54.4
|
1.0
|
C
|
E:HIS196
|
4.9
|
11.3
|
1.0
|
CD
|
E:GLU270
|
4.9
|
16.8
|
1.0
|
N
|
E:HIS69
|
4.9
|
9.0
|
1.0
|
CB
|
E:GLU72
|
5.0
|
9.6
|
1.0
|
|
Reference:
S.F.Wang,
J.-Y.Jin,
Z.H.Zeng,
G.R.Tian.
Optical 2-Benzyl-5-HYDROXY4OXOPENTANOIC Acids Against Carboxypeptidase A: Synthesis, Kinetic Evaluation and X-Ray Crystallographic Study Chin.Chem.Lett. V. 21 159 2010.
ISSN: ISSN 1001-8417
DOI: 10.1016/J.CCLET.2009.09.005
Page generated: Thu Oct 24 13:26:39 2024
|