6K0R
Ruvbl1-Ruvbl2 with truncated domain II in complex with phosphorylated Cordycepin
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 | 16 |
Details | binding site for residue ADP A 501 |
Chain | Residue |
A | SER17 |
A | LYS76 |
A | THR77 |
A | ALA78 |
A | TYR366 |
A | ILE374 |
A | LEU403 |
A | ARG404 |
A | HIS18 |
A | HIS20 |
A | GLY38 |
A | LEU39 |
A | VAL40 |
A | GLY73 |
A | THR74 |
A | GLY75 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue CUU B 501 |
Chain | Residue |
B | SER17 |
B | HIS18 |
B | HIS20 |
B | GLY38 |
B | LEU39 |
B | VAL40 |
B | GLY73 |
B | THR74 |
B | GLY75 |
B | LYS76 |
B | THR77 |
B | ALA78 |
B | TYR366 |
B | ILE374 |
B | LEU403 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue CUU C 501 |
Chain | Residue |
C | SER17 |
C | HIS18 |
C | HIS20 |
C | GLY38 |
C | LEU39 |
C | VAL40 |
C | PRO72 |
C | GLY73 |
C | THR74 |
C | GLY75 |
C | LYS76 |
C | THR77 |
C | ALA78 |
C | TYR366 |
C | ILE374 |
C | LEU403 |
site_id | AC4 |
Number of Residues | 14 |
Details | binding site for residue CUU D 501 |
Chain | Residue |
D | HIS27 |
D | MET46 |
D | VAL47 |
D | GLY80 |
D | THR81 |
D | GLY82 |
D | LYS83 |
D | THR84 |
D | ALA85 |
D | TYR362 |
D | ILE370 |
D | LEU399 |
D | ILE403 |
D | MG502 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue MG D 502 |
Chain | Residue |
D | CUU501 |
site_id | AC6 |
Number of Residues | 17 |
Details | binding site for residue 3AT E 501 |
Chain | Residue |
A | ASP356 |
E | ALA24 |
E | HIS27 |
E | GLY45 |
E | MET46 |
E | VAL47 |
E | GLY80 |
E | THR81 |
E | GLY82 |
E | LYS83 |
E | THR84 |
E | ALA85 |
E | ASP299 |
E | TYR362 |
E | ILE370 |
E | LEU399 |
E | ILE403 |
site_id | AC7 |
Number of Residues | 12 |
Details | binding site for residue CUU F 501 |
Chain | Residue |
F | ALA24 |
F | HIS25 |
F | HIS27 |
F | GLY45 |
F | MET46 |
F | VAL47 |
F | GLY80 |
F | THR81 |
F | GLY82 |
F | LYS83 |
F | THR84 |
F | TYR362 |
site_id | AC8 |
Number of Residues | 15 |
Details | binding site for residue CUU G 501 |
Chain | Residue |
G | GLY75 |
G | LYS76 |
G | THR77 |
G | ALA78 |
G | TYR366 |
G | ILE374 |
G | LEU403 |
G | SER17 |
G | HIS18 |
G | HIS20 |
G | GLY38 |
G | LEU39 |
G | VAL40 |
G | GLY73 |
G | THR74 |
site_id | AC9 |
Number of Residues | 14 |
Details | binding site for residue CUU H 501 |
Chain | Residue |
H | SER17 |
H | HIS18 |
H | HIS20 |
H | GLY38 |
H | LEU39 |
H | VAL40 |
H | GLY73 |
H | THR74 |
H | GLY75 |
H | LYS76 |
H | THR77 |
H | ASP302 |
H | TYR366 |
H | ILE374 |
site_id | AD1 |
Number of Residues | 16 |
Details | binding site for residue CUU I 501 |
Chain | Residue |
I | SER17 |
I | HIS18 |
I | HIS20 |
I | GLY38 |
I | LEU39 |
I | VAL40 |
I | PRO72 |
I | GLY73 |
I | THR74 |
I | GLY75 |
I | LYS76 |
I | THR77 |
I | ALA78 |
I | TYR366 |
I | ILE374 |
I | LEU403 |
site_id | AD2 |
Number of Residues | 15 |
Details | binding site for residue 3AT J 501 |
Chain | Residue |
J | HIS25 |
J | HIS27 |
J | GLY45 |
J | MET46 |
J | VAL47 |
J | GLN49 |
J | GLY80 |
J | THR81 |
J | GLY82 |
J | LYS83 |
J | THR84 |
J | ASP299 |
J | TYR362 |
J | LEU399 |
J | HOH601 |
site_id | AD3 |
Number of Residues | 14 |
Details | binding site for residue CUU K 501 |
Chain | Residue |
K | ALA24 |
K | HIS25 |
K | HIS27 |
K | GLY45 |
K | MET46 |
K | VAL47 |
K | GLY80 |
K | THR81 |
K | GLY82 |
K | LYS83 |
K | THR84 |
K | TYR362 |
K | ILE370 |
K | LEU399 |
site_id | AD4 |
Number of Residues | 10 |
Details | binding site for residue CU0 L 501 |
Chain | Residue |
L | HIS25 |
L | GLY80 |
L | THR81 |
L | GLY82 |
L | LYS83 |
L | THR84 |
L | ALA85 |
L | LEU399 |
L | ILE403 |
L | MG502 |
site_id | AD5 |
Number of Residues | 1 |
Details | binding site for residue MG L 502 |
Chain | Residue |
L | CU0501 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
D | GLY77 | |
E | GLY77 | |
F | GLY77 | |
J | GLY77 | |
K | GLY77 | |
L | GLY77 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.14, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 |
Chain | Residue | Details |
D | ALA2 | |
E | ALA2 | |
F | ALA2 | |
J | ALA2 | |
K | ALA2 | |
L | ALA2 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
D | SER437 | |
E | SER437 | |
F | SER437 | |
J | SER437 | |
K | SER437 | |
L | SER437 |
site_id | SWS_FT_FI4 |
Number of Residues | 24 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
D | LYS9 | |
H | LYS445 | |
F | LYS444 | |
F | LYS456 | |
J | LYS9 | |
J | LYS444 | |
J | LYS456 | |
K | LYS9 | |
K | LYS444 | |
A | LYS445 | |
K | LYS456 | |
L | LYS9 | |
L | LYS444 | |
L | LYS456 | |
D | LYS444 | |
D | LYS456 | |
E | LYS9 | |
C | LYS445 | |
E | LYS444 | |
E | LYS456 | |
F | LYS9 |