1GN1
crystal structure of the mouse CCT gamma apical domain (monoclinic)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
B | 0005524 | molecular_function | ATP binding |
B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
C | 0005524 | molecular_function | ATP binding |
C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
D | 0005524 | molecular_function | ATP binding |
D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
E | 0005524 | molecular_function | ATP binding |
E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
F | 0005524 | molecular_function | ATP binding |
F | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
G | 0005524 | molecular_function | ATP binding |
G | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
H | 0005524 | molecular_function | ATP binding |
H | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA F1378 |
Chain | Residue |
F | ASN221 |
F | GLU358 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA H1377 |
Chain | Residue |
C | GLU336 |
G | ASN221 |
H | ASN221 |
H | GLU358 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P49368 |
Chain | Residue | Details |
A | LYS222 | |
B | LYS222 | |
C | LYS222 | |
D | LYS222 | |
E | LYS222 | |
F | LYS222 | |
G | LYS222 | |
H | LYS222 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49368 |
Chain | Residue | Details |
A | SER243 | |
E | SER244 | |
F | SER243 | |
F | SER244 | |
G | SER243 | |
G | SER244 | |
H | SER243 | |
H | SER244 | |
A | SER244 | |
B | SER243 | |
B | SER244 | |
C | SER243 | |
C | SER244 | |
D | SER243 | |
D | SER244 | |
E | SER243 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P49368 |
Chain | Residue | Details |
A | TYR247 | |
B | TYR247 | |
C | TYR247 | |
D | TYR247 | |
E | TYR247 | |
F | TYR247 | |
G | TYR247 | |
H | TYR247 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
A | SER252 | |
B | SER252 | |
C | SER252 | |
D | SER252 | |
E | SER252 | |
F | SER252 | |
G | SER252 | |
H | SER252 |
site_id | SWS_FT_FI5 |
Number of Residues | 24 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P49368 |
Chain | Residue | Details |
A | LYS248 | |
D | LYS248 | |
D | LYS249 | |
E | LYS248 | |
E | LYS249 | |
F | LYS248 | |
F | LYS249 | |
G | LYS248 | |
G | LYS249 | |
H | LYS248 | |
H | LYS249 | |
A | LYS249 | |
B | LYS248 | |
B | LYS249 | |
C | LYS248 | |
C | LYS249 |