Zinc in PDB 2huc: Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants
Enzymatic activity of Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants
All present enzymatic activity of Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants:
3.1.4.3;
Protein crystallography data
The structure of Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants, PDB code: 2huc
was solved by
A.P.Benfield,
S.F.Martin,
N.M.Antikainen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
1.90
|
Space group
|
P 43 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
89.973,
89.973,
71.957,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.7 /
20.8
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants
(pdb code 2huc). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants, PDB code: 2huc:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 2huc
Go back to
Zinc Binding Sites List in 2huc
Zinc binding site 1 out
of 3 in the Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn246
b:15.4
occ:1.00
|
O
|
A:HOH249
|
2.1
|
12.6
|
1.0
|
ND1
|
A:HIS69
|
2.1
|
12.8
|
1.0
|
OD2
|
A:ASP122
|
2.2
|
11.9
|
1.0
|
NE2
|
A:HIS118
|
2.2
|
9.6
|
1.0
|
OD1
|
A:ASP55
|
2.4
|
10.8
|
1.0
|
CE1
|
A:HIS69
|
2.9
|
13.3
|
1.0
|
CG
|
A:ASP122
|
3.2
|
12.8
|
1.0
|
CE1
|
A:HIS118
|
3.2
|
11.1
|
1.0
|
CD2
|
A:HIS118
|
3.2
|
11.7
|
1.0
|
CG
|
A:ASP55
|
3.2
|
13.8
|
1.0
|
CG
|
A:HIS69
|
3.3
|
12.2
|
1.0
|
ZN
|
A:ZN248
|
3.3
|
15.5
|
1.0
|
OD2
|
A:ASP55
|
3.4
|
12.9
|
1.0
|
OD1
|
A:ASP122
|
3.4
|
11.4
|
1.0
|
O
|
A:HOH442
|
3.6
|
50.9
|
1.0
|
CB
|
A:HIS69
|
3.8
|
12.1
|
1.0
|
NE2
|
A:HIS14
|
4.0
|
10.9
|
1.0
|
NE2
|
A:HIS69
|
4.1
|
12.0
|
1.0
|
ND1
|
A:HIS118
|
4.3
|
11.0
|
1.0
|
CD2
|
A:HIS69
|
4.3
|
11.0
|
1.0
|
CG
|
A:HIS118
|
4.3
|
11.6
|
1.0
|
O
|
A:HOH250
|
4.4
|
18.2
|
1.0
|
CB
|
A:ASP122
|
4.5
|
11.3
|
1.0
|
CE1
|
A:HIS14
|
4.6
|
10.9
|
1.0
|
CB
|
A:ASP55
|
4.7
|
13.0
|
1.0
|
CE1
|
A:HIS128
|
4.7
|
13.9
|
1.0
|
CD2
|
A:HIS14
|
4.8
|
10.4
|
1.0
|
O
|
A:TRP1
|
4.9
|
11.9
|
1.0
|
CA
|
A:HIS69
|
5.0
|
11.6
|
1.0
|
|
Zinc binding site 2 out
of 3 in 2huc
Go back to
Zinc Binding Sites List in 2huc
Zinc binding site 2 out
of 3 in the Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn247
b:18.8
occ:1.00
|
NE2
|
A:HIS128
|
2.2
|
11.8
|
1.0
|
NE2
|
A:HIS142
|
2.2
|
15.3
|
1.0
|
O
|
A:HOH250
|
2.3
|
18.2
|
1.0
|
OE2
|
A:GLU146
|
2.4
|
12.0
|
1.0
|
O
|
A:HOH251
|
2.4
|
23.9
|
1.0
|
OE1
|
A:GLU146
|
2.5
|
16.4
|
1.0
|
CD
|
A:GLU146
|
2.7
|
15.6
|
1.0
|
CE1
|
A:HIS128
|
3.1
|
13.9
|
1.0
|
CE1
|
A:HIS142
|
3.2
|
15.2
|
1.0
|
CD2
|
A:HIS128
|
3.2
|
13.1
|
1.0
|
CD2
|
A:HIS142
|
3.2
|
15.0
|
1.0
|
O
|
A:HOH442
|
4.1
|
50.9
|
1.0
|
N
|
A:TRP1
|
4.1
|
10.3
|
1.0
|
CG
|
A:GLU146
|
4.1
|
14.7
|
1.0
|
ND1
|
A:HIS128
|
4.2
|
12.8
|
1.0
|
O
|
A:HOH338
|
4.2
|
27.1
|
1.0
|
ND1
|
A:HIS142
|
4.3
|
15.1
|
1.0
|
CG
|
A:HIS128
|
4.3
|
13.2
|
1.0
|
CG
|
A:HIS142
|
4.4
|
16.1
|
1.0
|
O
|
A:HOH259
|
4.5
|
23.8
|
1.0
|
OE1
|
A:GLN125
|
4.5
|
16.9
|
1.0
|
O
|
A:HOH249
|
4.5
|
12.6
|
1.0
|
ZN
|
A:ZN248
|
4.7
|
15.5
|
1.0
|
O
|
A:HOH256
|
4.9
|
35.4
|
1.0
|
CA
|
A:TRP1
|
4.9
|
12.4
|
1.0
|
O
|
A:TRP1
|
5.0
|
11.9
|
1.0
|
O
|
A:HOH254
|
5.0
|
34.4
|
1.0
|
|
Zinc binding site 3 out
of 3 in 2huc
Go back to
Zinc Binding Sites List in 2huc
Zinc binding site 3 out
of 3 in the Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structural Studies Examining the Substrate Specificity Profiles of Pc- Plcbc Protein Variants within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn248
b:15.5
occ:1.00
|
O
|
A:HOH249
|
2.1
|
12.6
|
1.0
|
NE2
|
A:HIS14
|
2.1
|
10.9
|
1.0
|
OD1
|
A:ASP122
|
2.2
|
11.4
|
1.0
|
N
|
A:TRP1
|
2.2
|
10.3
|
1.0
|
O
|
A:TRP1
|
2.3
|
11.9
|
1.0
|
C
|
A:TRP1
|
3.0
|
12.4
|
1.0
|
CD2
|
A:HIS14
|
3.0
|
10.4
|
1.0
|
O
|
A:HOH250
|
3.0
|
18.2
|
1.0
|
CA
|
A:TRP1
|
3.0
|
12.4
|
1.0
|
CG
|
A:ASP122
|
3.2
|
12.8
|
1.0
|
CE1
|
A:HIS14
|
3.2
|
10.9
|
1.0
|
ZN
|
A:ZN246
|
3.3
|
15.4
|
1.0
|
OD2
|
A:ASP122
|
3.5
|
11.9
|
1.0
|
CB
|
A:TRP1
|
3.7
|
11.0
|
1.0
|
OD2
|
A:ASP55
|
4.0
|
12.9
|
1.0
|
NE2
|
A:HIS118
|
4.0
|
9.6
|
1.0
|
CG
|
A:HIS14
|
4.2
|
10.1
|
1.0
|
ND1
|
A:HIS14
|
4.2
|
10.9
|
1.0
|
N
|
A:SER2
|
4.3
|
13.4
|
1.0
|
CE1
|
A:HIS118
|
4.3
|
11.1
|
1.0
|
CG
|
A:TRP1
|
4.4
|
14.1
|
1.0
|
CD1
|
A:TRP1
|
4.5
|
12.4
|
1.0
|
CE1
|
A:HIS128
|
4.5
|
13.9
|
1.0
|
CB
|
A:ASP122
|
4.5
|
11.3
|
1.0
|
NE2
|
A:HIS128
|
4.6
|
11.8
|
1.0
|
OE2
|
A:GLU146
|
4.6
|
12.0
|
1.0
|
ZN
|
A:ZN247
|
4.7
|
18.8
|
1.0
|
OD1
|
A:ASP55
|
4.7
|
10.8
|
1.0
|
CA
|
A:ASP122
|
4.8
|
10.5
|
1.0
|
CG
|
A:ASP55
|
4.8
|
13.8
|
1.0
|
O
|
A:HOH442
|
4.8
|
50.9
|
1.0
|
O
|
A:HOH338
|
4.9
|
27.1
|
1.0
|
CD2
|
A:HIS118
|
4.9
|
11.7
|
1.0
|
O
|
A:SER2
|
5.0
|
10.7
|
1.0
|
CA
|
A:SER2
|
5.0
|
13.4
|
1.0
|
|
Reference:
A.P.Benfield,
N.M.Goodey,
L.T.Phillips,
S.F.Martin.
Structural Studies Examining the Substrate Specificity Profiles of Pc-Plc(Bc) Protein Variants. Arch.Biochem.Biophys. V. 460 41 2007.
ISSN: ISSN 0003-9861
PubMed: 17324372
DOI: 10.1016/J.ABB.2007.01.023
Page generated: Thu Oct 17 00:42:54 2024
|