Calcium in PDB 5lq0: Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution
Protein crystallography data
The structure of Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution, PDB code: 5lq0
was solved by
P.Ecsedi,
G.Gogl,
B.Kiss,
L.Nyitray,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.77 /
2.90
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
56.450,
63.470,
268.910,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
22.7 /
26
|
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution
(pdb code 5lq0). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 6 binding sites of Calcium where determined in the
Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution, PDB code: 5lq0:
Jump to Calcium binding site number:
1;
2;
3;
4;
5;
6;
Calcium binding site 1 out
of 6 in 5lq0
Go back to
Calcium Binding Sites List in 5lq0
Calcium binding site 1 out
of 6 in the Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca401
b:71.1
occ:1.00
|
O
|
A:GLY282
|
2.5
|
72.1
|
1.0
|
OD1
|
A:ASP322
|
2.5
|
94.5
|
1.0
|
O
|
A:GLY280
|
2.7
|
0.8
|
1.0
|
OD2
|
A:ASP322
|
2.8
|
73.2
|
1.0
|
CG
|
A:ASP322
|
3.0
|
80.0
|
1.0
|
O
|
A:MET278
|
3.1
|
62.7
|
1.0
|
C
|
A:GLY282
|
3.6
|
78.1
|
1.0
|
N
|
A:GLY282
|
3.8
|
93.0
|
1.0
|
C
|
A:GLY280
|
4.0
|
0.8
|
1.0
|
C
|
A:MET278
|
4.1
|
66.5
|
1.0
|
CA
|
A:GLY282
|
4.2
|
82.2
|
1.0
|
OG1
|
A:THR283
|
4.2
|
74.3
|
1.0
|
C
|
A:LYS281
|
4.3
|
96.5
|
1.0
|
CB
|
A:ASP322
|
4.5
|
70.5
|
1.0
|
CA
|
A:MET278
|
4.5
|
63.9
|
1.0
|
CA
|
A:LYS281
|
4.6
|
95.0
|
1.0
|
N
|
A:THR283
|
4.7
|
78.6
|
1.0
|
N
|
A:LYS281
|
4.8
|
99.5
|
1.0
|
N
|
A:GLY280
|
4.8
|
0.9
|
1.0
|
C
|
A:LYS279
|
4.9
|
93.0
|
1.0
|
O
|
A:LYS281
|
5.0
|
97.3
|
1.0
|
CA
|
A:GLY280
|
5.0
|
0.2
|
1.0
|
|
Calcium binding site 2 out
of 6 in 5lq0
Go back to
Calcium Binding Sites List in 5lq0
Calcium binding site 2 out
of 6 in the Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca402
b:81.8
occ:1.00
|
OE1
|
A:GLU247
|
2.5
|
93.5
|
1.0
|
O
|
A:GLY207
|
2.6
|
0.8
|
1.0
|
O
|
A:ARG205
|
2.6
|
97.9
|
1.0
|
O
|
A:GLY202
|
2.8
|
79.2
|
1.0
|
OE2
|
A:GLU247
|
2.9
|
95.2
|
1.0
|
CD
|
A:GLU247
|
3.0
|
92.3
|
1.0
|
N
|
A:GLY207
|
3.2
|
98.6
|
1.0
|
C
|
A:GLY207
|
3.6
|
98.0
|
1.0
|
O
|
A:HOH501
|
3.6
|
49.1
|
1.0
|
CA
|
A:LYS206
|
3.7
|
94.2
|
1.0
|
C
|
A:ARG205
|
3.7
|
98.4
|
1.0
|
C
|
A:LYS206
|
3.8
|
99.7
|
1.0
|
C
|
A:GLY202
|
3.9
|
77.8
|
1.0
|
CA
|
A:GLY207
|
4.0
|
94.9
|
1.0
|
N
|
A:LYS206
|
4.2
|
97.5
|
1.0
|
CA
|
A:VAL203
|
4.3
|
73.3
|
1.0
|
O
|
A:VAL203
|
4.4
|
77.9
|
1.0
|
OG1
|
A:THR208
|
4.4
|
77.7
|
1.0
|
C
|
A:VAL203
|
4.5
|
76.9
|
1.0
|
CG
|
A:GLU247
|
4.5
|
88.7
|
1.0
|
N
|
A:VAL203
|
4.6
|
74.9
|
1.0
|
N
|
A:THR208
|
4.8
|
96.6
|
1.0
|
O
|
A:LYS206
|
4.8
|
0.9
|
1.0
|
CB
|
A:LYS206
|
4.9
|
90.1
|
1.0
|
CA
|
A:GLY202
|
5.0
|
76.9
|
1.0
|
CA
|
A:ARG205
|
5.0
|
0.5
|
1.0
|
|
Calcium binding site 3 out
of 6 in 5lq0
Go back to
Calcium Binding Sites List in 5lq0
Calcium binding site 3 out
of 6 in the Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca403
b:30.0
occ:1.00
|
OE1
|
A:GLU96
|
2.5
|
87.2
|
1.0
|
O
|
A:LEU91
|
2.8
|
78.1
|
1.0
|
CD
|
A:GLU96
|
3.1
|
81.1
|
1.0
|
OE2
|
A:GLU96
|
3.1
|
79.7
|
1.0
|
O
|
A:LYS88
|
3.3
|
91.4
|
1.0
|
CA
|
A:SER92
|
3.9
|
65.0
|
1.0
|
C
|
A:LEU91
|
3.9
|
71.0
|
1.0
|
CB
|
A:SER92
|
4.2
|
60.1
|
1.0
|
N
|
A:SER92
|
4.4
|
67.9
|
1.0
|
C
|
A:LYS88
|
4.5
|
84.4
|
1.0
|
CG
|
A:GLU96
|
4.5
|
72.6
|
1.0
|
|
Calcium binding site 4 out
of 6 in 5lq0
Go back to
Calcium Binding Sites List in 5lq0
Calcium binding site 4 out
of 6 in the Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca401
b:80.0
occ:1.00
|
O
|
B:ARG205
|
2.6
|
83.2
|
1.0
|
OE2
|
B:GLU247
|
2.6
|
96.2
|
1.0
|
OE1
|
B:GLU247
|
2.9
|
96.2
|
1.0
|
O
|
B:GLY207
|
3.0
|
83.2
|
1.0
|
CD
|
B:GLU247
|
3.1
|
93.9
|
1.0
|
O
|
B:GLY202
|
3.2
|
83.7
|
1.0
|
N
|
B:GLY207
|
3.5
|
97.4
|
1.0
|
C
|
B:ARG205
|
3.8
|
85.2
|
1.0
|
C
|
B:GLY207
|
4.0
|
87.7
|
1.0
|
CA
|
B:LYS206
|
4.1
|
94.7
|
1.0
|
O
|
B:VAL203
|
4.1
|
0.5
|
1.0
|
C
|
B:GLY202
|
4.2
|
85.0
|
1.0
|
C
|
B:LYS206
|
4.3
|
98.9
|
1.0
|
CA
|
B:GLY207
|
4.3
|
91.9
|
1.0
|
CA
|
B:VAL203
|
4.4
|
96.2
|
1.0
|
N
|
B:LYS206
|
4.4
|
89.8
|
1.0
|
C
|
B:VAL203
|
4.5
|
0.4
|
1.0
|
OG1
|
B:THR208
|
4.6
|
87.5
|
1.0
|
CG
|
B:GLU247
|
4.6
|
90.7
|
1.0
|
N
|
B:VAL203
|
4.8
|
87.0
|
1.0
|
CA
|
B:ARG205
|
4.9
|
84.2
|
1.0
|
|
Calcium binding site 5 out
of 6 in 5lq0
Go back to
Calcium Binding Sites List in 5lq0
Calcium binding site 5 out
of 6 in the Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 5 of Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca402
b:53.9
occ:1.00
|
O
|
B:GLY282
|
2.4
|
43.9
|
1.0
|
OD1
|
B:ASP322
|
2.5
|
70.5
|
1.0
|
O
|
B:GLY280
|
2.5
|
71.1
|
1.0
|
OD2
|
B:ASP322
|
2.5
|
61.5
|
1.0
|
O
|
B:MET278
|
2.6
|
52.9
|
1.0
|
CG
|
B:ASP322
|
2.8
|
60.9
|
1.0
|
C
|
B:MET278
|
3.6
|
58.8
|
1.0
|
C
|
B:GLY282
|
3.6
|
45.4
|
1.0
|
C
|
B:GLY280
|
3.7
|
68.0
|
1.0
|
N
|
B:GLY282
|
4.0
|
57.2
|
1.0
|
CA
|
B:MET278
|
4.0
|
55.2
|
1.0
|
OG1
|
B:THR283
|
4.2
|
47.4
|
1.0
|
C
|
B:LYS281
|
4.2
|
59.1
|
1.0
|
CB
|
B:ASP322
|
4.3
|
51.4
|
1.0
|
CA
|
B:GLY282
|
4.4
|
48.4
|
1.0
|
N
|
B:GLY280
|
4.5
|
64.3
|
1.0
|
CA
|
B:LYS281
|
4.5
|
63.7
|
1.0
|
N
|
B:LYS281
|
4.6
|
72.2
|
1.0
|
C
|
B:LYS279
|
4.6
|
54.3
|
1.0
|
CB
|
B:MET278
|
4.6
|
49.5
|
1.0
|
N
|
B:THR283
|
4.6
|
45.0
|
1.0
|
N
|
B:LYS279
|
4.7
|
62.5
|
1.0
|
CA
|
B:GLY280
|
4.7
|
70.2
|
1.0
|
O
|
B:LYS281
|
4.7
|
59.2
|
1.0
|
CA
|
B:THR283
|
4.8
|
45.0
|
1.0
|
O
|
B:LYS279
|
4.9
|
47.0
|
1.0
|
|
Calcium binding site 6 out
of 6 in 5lq0
Go back to
Calcium Binding Sites List in 5lq0
Calcium binding site 6 out
of 6 in the Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 6 of Crystal Structure of TYR24 Phosphorylated Annexin A2 at 2.9 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca403
b:0.6
occ:1.00
|
O
|
B:HOH502
|
2.6
|
38.9
|
1.0
|
O
|
B:GLY50
|
2.6
|
99.1
|
1.0
|
O
|
B:VAL51
|
2.7
|
81.7
|
1.0
|
OE1
|
B:GLU53
|
3.2
|
0.9
|
1.0
|
C
|
B:GLY50
|
3.6
|
97.5
|
1.0
|
C
|
B:VAL51
|
3.8
|
76.4
|
1.0
|
CD
|
B:GLU53
|
4.2
|
98.7
|
1.0
|
N
|
B:VAL51
|
4.4
|
91.7
|
1.0
|
CA
|
B:GLY50
|
4.4
|
0.9
|
1.0
|
CA
|
B:VAL51
|
4.5
|
81.5
|
1.0
|
OE2
|
B:GLU53
|
4.6
|
0.4
|
1.0
|
CB
|
B:VAL51
|
4.8
|
78.0
|
1.0
|
N
|
B:ASP52
|
4.9
|
69.1
|
1.0
|
N
|
B:GLU53
|
4.9
|
75.7
|
1.0
|
|
Reference:
P.Ecsedi,
B.Kiss,
G.Gogl,
L.Radnai,
L.Buday,
K.Koprivanacz,
K.Liliom,
I.Leveles,
B.Vertessy,
N.Jeszenoi,
C.Hetenyi,
G.Schlosser,
G.Katona,
L.Nyitray.
Regulation of the Equilibrium Between Closed and Open Conformations of Annexin A2 By N-Terminal Phosphorylation and S100A4-Binding. Structure V. 25 1195 2017.
ISSN: ISSN 1878-4186
PubMed: 28669632
DOI: 10.1016/J.STR.2017.06.001
Page generated: Mon Jul 15 07:45:16 2024
|