3UK6
Crystal Structure of the Tip48 (Tip49b) hexamer
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
A | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0005524 | molecular_function | ATP binding |
B | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
B | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0005524 | molecular_function | ATP binding |
C | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
C | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0005524 | molecular_function | ATP binding |
D | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
D | 0016887 | molecular_function | ATP hydrolysis activity |
E | 0005524 | molecular_function | ATP binding |
E | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
E | 0016887 | molecular_function | ATP hydrolysis activity |
F | 0005524 | molecular_function | ATP binding |
F | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
F | 0016887 | molecular_function | ATP hydrolysis activity |
G | 0005524 | molecular_function | ATP binding |
G | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
G | 0016887 | molecular_function | ATP hydrolysis activity |
H | 0005524 | molecular_function | ATP binding |
H | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
H | 0016887 | molecular_function | ATP hydrolysis activity |
I | 0005524 | molecular_function | ATP binding |
I | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
I | 0016887 | molecular_function | ATP hydrolysis activity |
J | 0005524 | molecular_function | ATP binding |
J | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
J | 0016887 | molecular_function | ATP hydrolysis activity |
K | 0005524 | molecular_function | ATP binding |
K | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
K | 0016887 | molecular_function | ATP hydrolysis activity |
L | 0005524 | molecular_function | ATP binding |
L | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
L | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADP A 1450 |
Chain | Residue |
A | ALA24 |
A | LYS83 |
A | THR84 |
A | ALA85 |
A | TYR362 |
A | LEU399 |
A | ILE403 |
A | HIS25 |
A | HIS27 |
A | GLY45 |
A | MET46 |
A | VAL47 |
A | GLY80 |
A | THR81 |
A | GLY82 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ADP B 1450 |
Chain | Residue |
B | ALA24 |
B | HIS25 |
B | HIS27 |
B | ILE28 |
B | GLY45 |
B | MET46 |
B | VAL47 |
B | GLY80 |
B | THR81 |
B | GLY82 |
B | LYS83 |
B | THR84 |
B | ALA85 |
B | TYR362 |
B | LEU399 |
B | ILE403 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ADP J 1450 |
Chain | Residue |
J | ALA24 |
J | HIS25 |
J | HIS27 |
J | GLY45 |
J | VAL47 |
J | PRO79 |
J | GLY80 |
J | THR81 |
J | GLY82 |
J | LYS83 |
J | THR84 |
J | ALA85 |
J | TYR362 |
J | ILE403 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ADP C 1450 |
Chain | Residue |
C | ALA24 |
C | HIS25 |
C | HIS27 |
C | GLY45 |
C | MET46 |
C | VAL47 |
C | GLY80 |
C | THR81 |
C | GLY82 |
C | LYS83 |
C | THR84 |
C | ALA85 |
C | TYR362 |
C | LEU399 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ADP I 1450 |
Chain | Residue |
I | ALA24 |
I | HIS25 |
I | HIS27 |
I | GLY45 |
I | MET46 |
I | VAL47 |
I | GLY80 |
I | THR81 |
I | GLY82 |
I | LYS83 |
I | THR84 |
I | ALA85 |
I | TYR362 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ADP D 1450 |
Chain | Residue |
D | ALA24 |
D | HIS25 |
D | HIS27 |
D | GLY45 |
D | MET46 |
D | VAL47 |
D | GLY80 |
D | THR81 |
D | GLY82 |
D | LYS83 |
D | THR84 |
D | ALA85 |
D | TYR362 |
D | ILE370 |
D | LEU399 |
D | ILE403 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADP H 1450 |
Chain | Residue |
H | ALA85 |
H | TYR362 |
H | LEU399 |
H | ILE403 |
H | ALA24 |
H | HIS25 |
H | HIS27 |
H | GLY45 |
H | MET46 |
H | VAL47 |
H | GLY80 |
H | THR81 |
H | GLY82 |
H | LYS83 |
H | THR84 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADP F 1450 |
Chain | Residue |
F | ALA24 |
F | HIS25 |
F | HIS27 |
F | GLY45 |
F | VAL47 |
F | GLY80 |
F | THR81 |
F | GLY82 |
F | LYS83 |
F | THR84 |
F | ALA85 |
F | TYR362 |
F | ILE370 |
F | LEU399 |
F | ILE403 |
site_id | AC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ADP K 1450 |
Chain | Residue |
K | ALA24 |
K | HIS25 |
K | HIS27 |
K | ILE28 |
K | GLY45 |
K | MET46 |
K | VAL47 |
K | THR81 |
K | GLY82 |
K | LYS83 |
K | THR84 |
K | ALA85 |
K | TYR362 |
K | ILE403 |
site_id | BC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ADP E 1450 |
Chain | Residue |
E | ALA24 |
E | HIS25 |
E | HIS27 |
E | GLY45 |
E | MET46 |
E | VAL47 |
E | GLY80 |
E | THR81 |
E | GLY82 |
E | LYS83 |
E | THR84 |
E | ALA85 |
E | TYR362 |
E | ILE370 |
E | LEU399 |
E | ILE403 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ADP L 1450 |
Chain | Residue |
L | GLY80 |
L | THR81 |
L | GLY82 |
L | LYS83 |
L | THR84 |
L | ALA85 |
L | TYR362 |
L | LEU399 |
site_id | BC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ADP G 1450 |
Chain | Residue |
G | ALA24 |
G | HIS25 |
G | HIS27 |
G | GLY45 |
G | MET46 |
G | VAL47 |
G | GLY80 |
G | THR81 |
G | GLY82 |
G | LYS83 |
G | THR84 |
G | ALA85 |
G | TYR362 |
G | ILE370 |
G | LEU399 |
G | ILE403 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY77 | |
J | GLY77 | |
K | GLY77 | |
L | GLY77 | |
B | GLY77 | |
C | GLY77 | |
D | GLY77 | |
E | GLY77 | |
F | GLY77 | |
G | GLY77 | |
H | GLY77 | |
I | GLY77 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.14, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 |
Chain | Residue | Details |
A | ALA2 | |
J | ALA2 | |
K | ALA2 | |
L | ALA2 | |
B | ALA2 | |
C | ALA2 | |
D | ALA2 | |
E | ALA2 | |
F | ALA2 | |
G | ALA2 | |
H | ALA2 | |
I | ALA2 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER437 | |
J | SER437 | |
K | SER437 | |
L | SER437 | |
B | SER437 | |
C | SER437 | |
D | SER437 | |
E | SER437 | |
F | SER437 | |
G | SER437 | |
H | SER437 | |
I | SER437 |
site_id | SWS_FT_FI4 |
Number of Residues | 48 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS9 | |
C | LYS444 | |
C | LYS456 | |
D | LYS9 | |
D | LYS444 | |
D | LYS456 | |
E | LYS9 | |
E | LYS444 | |
E | LYS456 | |
F | LYS9 | |
F | LYS444 | |
F | LYS456 | |
G | LYS9 | |
G | LYS444 | |
G | LYS456 | |
H | LYS9 | |
A | LYS444 | |
H | LYS444 | |
H | LYS456 | |
I | LYS9 | |
I | LYS444 | |
I | LYS456 | |
J | LYS9 | |
J | LYS444 | |
A | LYS456 | |
J | LYS456 | |
K | LYS9 | |
K | LYS444 | |
K | LYS456 | |
L | LYS9 | |
L | LYS444 | |
L | LYS456 | |
B | LYS9 | |
B | LYS444 | |
B | LYS456 | |
C | LYS9 |