Aluminium in PDB 5lih: Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain
Enzymatic activity of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain
All present enzymatic activity of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain:
2.7.11.13;
Protein crystallography data
The structure of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain, PDB code: 5lih
was solved by
E.V.Soriano,
A.G.Purkiss,
N.Q.Mcdonald,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
67.28 /
3.25
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
78.980,
84.230,
111.830,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
25.7 /
28.4
|
Other elements in 5lih:
The structure of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain also contains other interesting chemical elements:
Aluminium Binding Sites:
The binding sites of Aluminium atom in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain
(pdb code 5lih). This binding sites where shown within
5.0 Angstroms radius around Aluminium atom.
In total 4 binding sites of Aluminium where determined in the
Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain, PDB code: 5lih:
Jump to Aluminium binding site number:
1;
2;
3;
4;
Aluminium binding site 1 out
of 4 in 5lih
Go back to
Aluminium Binding Sites List in 5lih
Aluminium binding site 1 out
of 4 in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain
 Mono view
 Stereo pair view
|
A full contact list of Aluminium with other atoms in the Al binding
site number 1 of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Al602
b:37.9
occ:1.00
|
AL
|
A:AF3602
|
0.0
|
37.9
|
1.0
|
F3
|
A:AF3602
|
1.8
|
37.9
|
1.0
|
F2
|
A:AF3602
|
1.8
|
37.9
|
1.0
|
F1
|
A:AF3602
|
1.8
|
37.9
|
1.0
|
O
|
A:TYR419
|
3.4
|
29.4
|
1.0
|
O
|
A:ARG377
|
3.9
|
31.5
|
1.0
|
C
|
A:ARG377
|
3.9
|
31.8
|
1.0
|
O
|
A:VAL434
|
4.0
|
31.7
|
1.0
|
C
|
A:TYR419
|
4.1
|
29.4
|
1.0
|
CA
|
A:ARG377
|
4.2
|
33.3
|
1.0
|
CA
|
A:ILE420
|
4.2
|
31.1
|
1.0
|
CB
|
A:ALA438
|
4.3
|
27.8
|
1.0
|
N
|
A:ASP378
|
4.5
|
30.6
|
1.0
|
N
|
A:ILE420
|
4.5
|
30.8
|
1.0
|
CB
|
A:TYR419
|
4.6
|
29.8
|
1.0
|
N
|
A:ALA421
|
4.6
|
26.0
|
1.0
|
CB
|
A:VAL434
|
4.7
|
35.1
|
1.0
|
CA
|
A:GLY415
|
4.7
|
34.2
|
1.0
|
CD1
|
A:ILE424
|
4.8
|
35.2
|
1.0
|
O
|
A:CYS414
|
4.8
|
35.9
|
1.0
|
C
|
A:VAL434
|
4.8
|
33.1
|
1.0
|
CA
|
A:ASP378
|
4.9
|
30.1
|
1.0
|
C
|
A:ILE420
|
4.9
|
31.6
|
1.0
|
CB
|
A:ARG377
|
4.9
|
34.8
|
1.0
|
CG2
|
A:VAL434
|
5.0
|
35.9
|
1.0
|
|
Aluminium binding site 2 out
of 4 in 5lih
Go back to
Aluminium Binding Sites List in 5lih
Aluminium binding site 2 out
of 4 in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain
 Mono view
 Stereo pair view
|
A full contact list of Aluminium with other atoms in the Al binding
site number 2 of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Al605
b:54.5
occ:1.00
|
AL
|
A:AF3605
|
0.0
|
54.5
|
1.0
|
F3
|
A:AF3605
|
1.8
|
34.8
|
1.0
|
F1
|
A:AF3605
|
1.8
|
22.1
|
1.0
|
F2
|
A:AF3605
|
1.8
|
63.9
|
1.0
|
O1B
|
A:ADP601
|
2.4
|
40.8
|
1.0
|
OD2
|
A:ASP396
|
3.0
|
34.3
|
1.0
|
OG
|
F:SER11
|
3.2
|
43.9
|
1.0
|
PB
|
A:ADP601
|
3.4
|
45.0
|
1.0
|
O2B
|
A:ADP601
|
3.4
|
43.8
|
1.0
|
MN
|
A:MN603
|
3.6
|
31.8
|
1.0
|
MN
|
A:MN604
|
3.6
|
38.7
|
1.0
|
CB
|
F:SER11
|
3.8
|
43.2
|
1.0
|
N
|
F:SER11
|
3.8
|
41.5
|
1.0
|
OG
|
A:SER264
|
4.0
|
37.6
|
1.0
|
O1A
|
A:ADP601
|
4.1
|
33.5
|
1.0
|
CE
|
A:LYS380
|
4.1
|
31.4
|
1.0
|
CG
|
A:ASP396
|
4.1
|
34.4
|
1.0
|
OD2
|
A:ASP378
|
4.2
|
30.9
|
1.0
|
O3B
|
A:ADP601
|
4.3
|
58.6
|
1.0
|
CA
|
F:SER11
|
4.4
|
42.2
|
1.0
|
N
|
A:SER264
|
4.5
|
36.9
|
1.0
|
OD1
|
A:ASP396
|
4.6
|
34.5
|
1.0
|
O3A
|
A:ADP601
|
4.6
|
36.4
|
1.0
|
OD1
|
A:ASN383
|
4.7
|
31.2
|
0.5
|
OD1
|
A:ASN383
|
4.7
|
31.2
|
0.5
|
CA
|
F:GLY10
|
4.8
|
40.5
|
1.0
|
C
|
F:GLY10
|
4.8
|
40.8
|
1.0
|
CA
|
A:GLY263
|
4.9
|
36.4
|
1.0
|
|
Aluminium binding site 3 out
of 4 in 5lih
Go back to
Aluminium Binding Sites List in 5lih
Aluminium binding site 3 out
of 4 in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain
 Mono view
 Stereo pair view
|
A full contact list of Aluminium with other atoms in the Al binding
site number 3 of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Al602
b:36.8
occ:1.00
|
AL
|
B:AF3602
|
0.0
|
36.8
|
1.0
|
F3
|
B:AF3602
|
1.8
|
36.8
|
1.0
|
F2
|
B:AF3602
|
1.8
|
36.8
|
1.0
|
F1
|
B:AF3602
|
1.8
|
36.8
|
1.0
|
C
|
B:ARG377
|
3.6
|
42.0
|
1.0
|
O
|
B:ARG377
|
3.7
|
43.1
|
1.0
|
O
|
B:TYR419
|
3.7
|
40.7
|
1.0
|
O
|
B:VAL434
|
3.9
|
35.1
|
1.0
|
CA
|
B:ARG377
|
3.9
|
42.5
|
1.0
|
N
|
B:ASP378
|
4.1
|
40.7
|
1.0
|
CB
|
B:ALA438
|
4.2
|
31.6
|
1.0
|
C
|
B:TYR419
|
4.3
|
41.0
|
1.0
|
CG
|
B:ARG377
|
4.4
|
46.0
|
1.0
|
CA
|
B:ASP378
|
4.5
|
40.5
|
1.0
|
CB
|
B:TYR419
|
4.6
|
39.0
|
1.0
|
CB
|
B:VAL434
|
4.6
|
37.3
|
1.0
|
C
|
B:VAL434
|
4.7
|
35.1
|
1.0
|
CA
|
B:ILE420
|
4.7
|
37.5
|
1.0
|
N
|
B:LEU379
|
4.7
|
35.6
|
1.0
|
CB
|
B:ARG377
|
4.8
|
44.2
|
1.0
|
N
|
B:ILE420
|
4.8
|
36.6
|
1.0
|
CA
|
B:GLY415
|
4.8
|
44.9
|
1.0
|
CG2
|
B:VAL434
|
4.8
|
36.9
|
1.0
|
N
|
B:ARG377
|
5.0
|
41.3
|
1.0
|
|
Aluminium binding site 4 out
of 4 in 5lih
Go back to
Aluminium Binding Sites List in 5lih
Aluminium binding site 4 out
of 4 in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain
 Mono view
 Stereo pair view
|
A full contact list of Aluminium with other atoms in the Al binding
site number 4 of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Al605
b:59.4
occ:1.00
|
AL
|
B:AF3605
|
0.0
|
59.4
|
1.0
|
F1
|
B:AF3605
|
1.8
|
26.9
|
1.0
|
F2
|
B:AF3605
|
1.8
|
68.7
|
1.0
|
F3
|
B:AF3605
|
1.8
|
39.6
|
1.0
|
O1B
|
B:ADP601
|
2.4
|
44.1
|
1.0
|
MN
|
B:MN604
|
2.9
|
40.7
|
1.0
|
OG
|
G:SER11
|
3.1
|
48.4
|
1.0
|
PB
|
B:ADP601
|
3.5
|
38.5
|
1.0
|
CB
|
G:SER11
|
3.5
|
46.9
|
1.0
|
OD2
|
B:ASP396
|
3.6
|
41.9
|
1.0
|
N
|
G:SER11
|
3.6
|
44.5
|
1.0
|
MN
|
B:MN603
|
3.6
|
50.6
|
1.0
|
N
|
B:SER264
|
3.9
|
43.9
|
1.0
|
O3B
|
B:ADP601
|
4.0
|
46.1
|
1.0
|
O2B
|
B:ADP601
|
4.1
|
38.3
|
1.0
|
CA
|
G:SER11
|
4.2
|
45.3
|
1.0
|
CB
|
B:SER264
|
4.3
|
46.3
|
1.0
|
CE
|
B:LYS380
|
4.4
|
39.0
|
1.0
|
O1A
|
B:ADP601
|
4.5
|
46.0
|
1.0
|
OD2
|
B:ASP378
|
4.5
|
41.2
|
1.0
|
CA
|
B:GLY263
|
4.6
|
42.2
|
1.0
|
C
|
G:GLY10
|
4.6
|
50.4
|
1.0
|
CG
|
B:ASP396
|
4.7
|
41.8
|
1.0
|
CA
|
B:SER264
|
4.7
|
45.5
|
1.0
|
CA
|
G:GLY10
|
4.7
|
50.1
|
1.0
|
C
|
B:GLY263
|
4.7
|
43.8
|
1.0
|
O3A
|
B:ADP601
|
4.8
|
45.9
|
1.0
|
O
|
B:HOH705
|
4.9
|
37.6
|
1.0
|
|
Reference:
E.V.Soriano,
M.E.Ivanova,
G.Fletcher,
P.Riou,
P.P.Knowles,
K.Barnouin,
A.Purkiss,
B.Kostelecky,
P.Saiu,
M.Linch,
A.Elbediwy,
S.Kjr,
N.O'reilly,
A.P.Snijders,
P.J.Parker,
B.J.Thompson,
N.Q.Mcdonald.
Apkc Inhibition By PAR3 CR3 Flanking Regions Controls Substrate Access and Underpins Apical-Junctional Polarization. Dev.Cell V. 38 384 2016.
ISSN: ISSN 1534-5807
PubMed: 27554858
DOI: 10.1016/J.DEVCEL.2016.07.018
Page generated: Wed Jul 10 09:50:37 2024
|