8OH2
Structure of the Tau-PAM4 Type 1 amyloid fibril
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0015631 | molecular_function | tubulin binding |
B | 0015631 | molecular_function | tubulin binding |
C | 0015631 | molecular_function | tubulin binding |
D | 0015631 | molecular_function | tubulin binding |
E | 0015631 | molecular_function | tubulin binding |
F | 0015631 | molecular_function | tubulin binding |
G | 0015631 | molecular_function | tubulin binding |
H | 0015631 | molecular_function | tubulin binding |
I | 0015631 | molecular_function | tubulin binding |
J | 0015631 | molecular_function | tubulin binding |
K | 0015631 | molecular_function | tubulin binding |
L | 0015631 | molecular_function | tubulin binding |
M | 0015631 | molecular_function | tubulin binding |
N | 0015631 | molecular_function | tubulin binding |
O | 0015631 | molecular_function | tubulin binding |
P | 0015631 | molecular_function | tubulin binding |
Q | 0015631 | molecular_function | tubulin binding |
R | 0015631 | molecular_function | tubulin binding |
S | 0015631 | molecular_function | tubulin binding |
T | 0015631 | molecular_function | tubulin binding |
U | 0015631 | molecular_function | tubulin binding |
V | 0015631 | molecular_function | tubulin binding |
W | 0015631 | molecular_function | tubulin binding |
X | 0015631 | molecular_function | tubulin binding |
Y | 0015631 | molecular_function | tubulin binding |
Z | 0015631 | molecular_function | tubulin binding |
a | 0015631 | molecular_function | tubulin binding |
b | 0015631 | molecular_function | tubulin binding |
c | 0015631 | molecular_function | tubulin binding |
d | 0015631 | molecular_function | tubulin binding |
e | 0015631 | molecular_function | tubulin binding |
f | 0015631 | molecular_function | tubulin binding |
g | 0015631 | molecular_function | tubulin binding |
h | 0015631 | molecular_function | tubulin binding |
i | 0015631 | molecular_function | tubulin binding |
j | 0015631 | molecular_function | tubulin binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 36 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P10637 |
Chain | Residue | Details |
A | ACE349 | |
J | ACE349 | |
K | ACE349 | |
L | ACE349 | |
M | ACE349 | |
N | ACE349 | |
O | ACE349 | |
P | ACE349 | |
Q | ACE349 | |
R | ACE349 | |
S | ACE349 | |
B | ACE349 | |
T | ACE349 | |
U | ACE349 | |
V | ACE349 | |
W | ACE349 | |
X | ACE349 | |
Y | ACE349 | |
Z | ACE349 | |
a | ACE349 | |
b | ACE349 | |
c | ACE349 | |
C | ACE349 | |
d | ACE349 | |
e | ACE349 | |
f | ACE349 | |
g | ACE349 | |
h | ACE349 | |
i | ACE349 | |
j | ACE349 | |
D | ACE349 | |
E | ACE349 | |
F | ACE349 | |
G | ACE349 | |
H | ACE349 | |
I | ACE349 |
site_id | SWS_FT_FI2 |
Number of Residues | 36 |
Details | MOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:8999860 |
Chain | Residue | Details |
A | SER352 | |
J | SER352 | |
K | SER352 | |
L | SER352 | |
M | SER352 | |
N | SER352 | |
O | SER352 | |
P | SER352 | |
Q | SER352 | |
R | SER352 | |
S | SER352 | |
B | SER352 | |
T | SER352 | |
U | SER352 | |
V | SER352 | |
W | SER352 | |
X | SER352 | |
Y | SER352 | |
Z | SER352 | |
a | SER352 | |
b | SER352 | |
c | SER352 | |
C | SER352 | |
d | SER352 | |
e | SER352 | |
f | SER352 | |
g | SER352 | |
h | SER352 | |
i | SER352 | |
j | SER352 | |
D | SER352 | |
E | SER352 | |
F | SER352 | |
G | SER352 | |
H | SER352 | |
I | SER352 |
site_id | SWS_FT_FI3 |
Number of Residues | 36 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:7706316 |
Chain | Residue | Details |
A | SER356 | |
J | SER356 | |
K | SER356 | |
L | SER356 | |
M | SER356 | |
N | SER356 | |
O | SER356 | |
P | SER356 | |
Q | SER356 | |
R | SER356 | |
S | SER356 | |
B | SER356 | |
T | SER356 | |
U | SER356 | |
V | SER356 | |
W | SER356 | |
X | SER356 | |
Y | SER356 | |
Z | SER356 | |
a | SER356 | |
b | SER356 | |
c | SER356 | |
C | SER356 | |
d | SER356 | |
e | SER356 | |
f | SER356 | |
g | SER356 | |
h | SER356 | |
i | SER356 | |
j | SER356 | |
D | SER356 | |
E | SER356 | |
F | SER356 | |
G | SER356 | |
H | SER356 | |
I | SER356 |
site_id | SWS_FT_FI4 |
Number of Residues | 36 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300 |
Chain | Residue | Details |
A | LYS353 | |
J | LYS353 | |
K | LYS353 | |
L | LYS353 | |
M | LYS353 | |
N | LYS353 | |
O | LYS353 | |
P | LYS353 | |
Q | LYS353 | |
R | LYS353 | |
S | LYS353 | |
B | LYS353 | |
T | LYS353 | |
U | LYS353 | |
V | LYS353 | |
W | LYS353 | |
X | LYS353 | |
Y | LYS353 | |
Z | LYS353 | |
a | LYS353 | |
b | LYS353 | |
c | LYS353 | |
C | LYS353 | |
d | LYS353 | |
e | LYS353 | |
f | LYS353 | |
g | LYS353 | |
h | LYS353 | |
i | LYS353 | |
j | LYS353 | |
D | LYS353 | |
E | LYS353 | |
F | LYS353 | |
G | LYS353 | |
H | LYS353 | |
I | LYS353 |
site_id | SWS_FT_FI5 |
Number of Residues | 72 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau => ECO:0000269|PubMed:16443603 |
Chain | Residue | Details |
A | LYS353 | |
F | LYS353 | |
G | LYS353 | |
H | LYS353 | |
I | LYS353 | |
J | LYS353 | |
K | LYS353 | |
L | LYS353 | |
M | LYS353 | |
N | LYS353 | |
O | LYS353 | |
B | LYS353 | |
P | LYS353 | |
Q | LYS353 | |
R | LYS353 | |
S | LYS353 | |
T | LYS353 | |
U | LYS353 | |
V | LYS353 | |
W | LYS353 | |
X | LYS353 | |
Y | LYS353 | |
C | LYS353 | |
Z | LYS353 | |
a | LYS353 | |
b | LYS353 | |
c | LYS353 | |
d | LYS353 | |
e | LYS353 | |
f | LYS353 | |
g | LYS353 | |
h | LYS353 | |
i | LYS353 | |
D | LYS353 | |
j | LYS353 | |
E | LYS353 |