6HK6
Human RIOK2 bound to inhibitor
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004674 | molecular_function | protein serine/threonine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004672 | molecular_function | protein kinase activity |
D | 0004674 | molecular_function | protein serine/threonine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
E | 0004672 | molecular_function | protein kinase activity |
E | 0004674 | molecular_function | protein serine/threonine kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006468 | biological_process | protein phosphorylation |
F | 0004672 | molecular_function | protein kinase activity |
F | 0004674 | molecular_function | protein serine/threonine kinase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006468 | biological_process | protein phosphorylation |
G | 0004672 | molecular_function | protein kinase activity |
G | 0004674 | molecular_function | protein serine/threonine kinase activity |
G | 0005524 | molecular_function | ATP binding |
G | 0006468 | biological_process | protein phosphorylation |
H | 0004672 | molecular_function | protein kinase activity |
H | 0004674 | molecular_function | protein serine/threonine kinase activity |
H | 0005524 | molecular_function | ATP binding |
H | 0006468 | biological_process | protein phosphorylation |
I | 0004672 | molecular_function | protein kinase activity |
I | 0004674 | molecular_function | protein serine/threonine kinase activity |
I | 0005524 | molecular_function | ATP binding |
I | 0006468 | biological_process | protein phosphorylation |
J | 0004672 | molecular_function | protein kinase activity |
J | 0004674 | molecular_function | protein serine/threonine kinase activity |
J | 0005524 | molecular_function | ATP binding |
J | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue G8H A 401 |
Chain | Residue |
A | MET101 |
A | ILE111 |
A | ALA121 |
A | GLU189 |
A | ILE191 |
A | GLY193 |
A | ILE235 |
A | ILE245 |
F | HIS200 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue CL A 402 |
Chain | Residue |
A | ARG14 |
A | ARG18 |
H | HIS200 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | ASP81 |
A | VAL97 |
A | TYR110 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | ASN77 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | SER107 |
A | ASP108 |
A | ARG129 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue G8H B 401 |
Chain | Residue |
B | MET101 |
B | ALA121 |
B | GLU189 |
B | LEU190 |
B | ILE191 |
B | GLY193 |
B | ILE235 |
B | ILE245 |
I | HIS200 |
I | ARG276 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue EPE B 402 |
Chain | Residue |
B | ARG171 |
B | HIS222 |
B | GLU293 |
B | ASP294 |
B | THR295 |
C | ASP294 |
C | THR295 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue EDO B 403 |
Chain | Residue |
B | ASP81 |
B | VAL97 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
A | ASP271 |
B | TRP260 |
B | ASP263 |
B | LYS267 |
B | HOH521 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
A | TRP260 |
A | ASP263 |
A | LYS267 |
B | CYS268 |
B | ASP271 |
B | LYS275 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue G8H C 401 |
Chain | Residue |
C | MET101 |
C | ILE111 |
C | ALA121 |
C | GLU189 |
C | ILE191 |
C | GLY193 |
C | ILE235 |
C | ILE245 |
D | HIS200 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue G8H D 401 |
Chain | Residue |
C | HIS200 |
D | MET101 |
D | ILE111 |
D | ALA121 |
D | GLU189 |
D | ILE191 |
D | GLY193 |
D | ILE235 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue EPE D 402 |
Chain | Residue |
D | HIS222 |
D | GLU293 |
D | ASP294 |
D | THR295 |
G | GLU293 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue G8H E 401 |
Chain | Residue |
E | MET101 |
E | ILE111 |
E | ALA121 |
E | GLU189 |
E | ILE191 |
E | GLY193 |
E | ILE235 |
J | HIS200 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue EPE E 402 |
Chain | Residue |
E | ARG171 |
E | HIS222 |
E | GLU293 |
E | ASP294 |
E | THR295 |
F | THR295 |
site_id | AD7 |
Number of Residues | 9 |
Details | binding site for residue G8H F 401 |
Chain | Residue |
A | HIS200 |
F | MET101 |
F | ILE109 |
F | ILE111 |
F | ALA121 |
F | GLU189 |
F | ILE191 |
F | GLY193 |
F | ILE235 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue EDO F 402 |
Chain | Residue |
F | ASP81 |
F | VAL97 |
F | TYR110 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue G8H G 600 |
Chain | Residue |
G | ILE191 |
G | GLY193 |
G | ILE235 |
G | ALA121 |
G | GLU189 |
site_id | AE1 |
Number of Residues | 9 |
Details | binding site for residue G8H H 401 |
Chain | Residue |
A | LYS45 |
H | MET101 |
H | ILE111 |
H | ALA121 |
H | GLU189 |
H | ILE191 |
H | GLY193 |
H | ILE235 |
H | ILE245 |
site_id | AE2 |
Number of Residues | 2 |
Details | binding site for residue EPE H 402 |
Chain | Residue |
H | GLU293 |
H | THR295 |
site_id | AE3 |
Number of Residues | 1 |
Details | binding site for residue CL H 403 |
Chain | Residue |
H | TYR164 |
site_id | AE4 |
Number of Residues | 8 |
Details | binding site for residue G8H I 600 |
Chain | Residue |
B | HIS200 |
I | MET101 |
I | ILE111 |
I | ALA121 |
I | GLU189 |
I | ILE191 |
I | GLY193 |
I | ILE235 |
site_id | AE5 |
Number of Residues | 8 |
Details | binding site for residue G8H J 600 |
Chain | Residue |
E | HIS200 |
J | MET101 |
J | ILE111 |
J | ALA121 |
J | GLU189 |
J | ILE191 |
J | GLY193 |
J | ILE235 |
Functional Information from PROSITE/UniProt
site_id | PS01245 |
Number of Residues | 12 |
Details | RIO1 RIO1/ZK632.3/MJ0444 family signature. LIHGDFNEFNlI |
Chain | Residue | Details |
A | LEU224-ILE235 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | ASP228 | |
J | ASP228 | |
B | ASP228 | |
C | ASP228 | |
D | ASP228 | |
E | ASP228 | |
F | ASP228 | |
G | ASP228 | |
H | ASP228 | |
I | ASP228 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | LYS123 | |
J | LYS123 | |
B | LYS123 | |
C | LYS123 | |
D | LYS123 | |
E | LYS123 | |
F | LYS123 | |
G | LYS123 | |
H | LYS123 | |
I | LYS123 |