3QXY
Human SETD6 in complex with RelA Lys310
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| A | 0018022 | biological_process | peptidyl-lysine methylation |
| A | 0018026 | biological_process | peptidyl-lysine monomethylation |
| A | 0019827 | biological_process | stem cell population maintenance |
| A | 0032088 | biological_process | negative regulation of NF-kappaB transcription factor activity |
| A | 0032259 | biological_process | methylation |
| A | 0048863 | biological_process | stem cell differentiation |
| A | 0050727 | biological_process | regulation of inflammatory response |
| A | 0051059 | molecular_function | NF-kappaB binding |
| A | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| B | 0018022 | biological_process | peptidyl-lysine methylation |
| B | 0018026 | biological_process | peptidyl-lysine monomethylation |
| B | 0019827 | biological_process | stem cell population maintenance |
| B | 0032088 | biological_process | negative regulation of NF-kappaB transcription factor activity |
| B | 0032259 | biological_process | methylation |
| B | 0048863 | biological_process | stem cell differentiation |
| B | 0050727 | biological_process | regulation of inflammatory response |
| B | 0051059 | molecular_function | NF-kappaB binding |
| B | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SAM A 6734 |
| Chain | Residue |
| A | ALA73 |
| A | HIS252 |
| A | TYR285 |
| A | TYR297 |
| A | PHE299 |
| A | EDO480 |
| A | HOH533 |
| A | HOH568 |
| A | HOH580 |
| A | HOH606 |
| A | HOH652 |
| A | GLY74 |
| A | HOH668 |
| P | LYS310 |
| A | TYR75 |
| A | ALA222 |
| A | TYR223 |
| A | ASP248 |
| A | ILE249 |
| A | LEU250 |
| A | ASN251 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 474 |
| Chain | Residue |
| A | LEU150 |
| A | GLY151 |
| A | ARG152 |
| A | LEU153 |
| A | PHE158 |
| A | GLN215 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 475 |
| Chain | Residue |
| A | SER120 |
| A | ASN183 |
| A | GLU187 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 476 |
| Chain | Residue |
| A | LEU424 |
| A | TYR427 |
| A | ALA428 |
| A | THR429 |
| A | HOH532 |
| A | HOH765 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 477 |
| Chain | Residue |
| A | THR368 |
| A | GLU396 |
| A | GLU397 |
| A | GLY398 |
| A | SER399 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 478 |
| Chain | Residue |
| A | VAL300 |
| A | TYR444 |
| A | TRP449 |
| A | GLN452 |
| A | HOH626 |
| A | HOH722 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 479 |
| Chain | Residue |
| A | ARG30 |
| A | LEU34 |
| A | LEU36 |
| A | HOH573 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 480 |
| Chain | Residue |
| A | HOH46 |
| A | LEU253 |
| A | VAL300 |
| A | HOH626 |
| A | HOH641 |
| A | SAM6734 |
| B | LYS441 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 481 |
| Chain | Residue |
| A | ASN440 |
| A | GLU442 |
| B | ARG68 |
| B | GLY74 |
| B | EDO477 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 482 |
| Chain | Residue |
| A | LEU362 |
| A | THR363 |
| A | GLU364 |
| A | GLU365 |
| A | GLU366 |
| A | HOH676 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 483 |
| Chain | Residue |
| A | GLN324 |
| A | ASN418 |
| A | LEU421 |
| A | LEU422 |
| A | GLN425 |
| A | HOH584 |
| A | HOH605 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 484 |
| Chain | Residue |
| A | GLU161 |
| A | ARG165 |
| A | GLU178 |
| A | HOH780 |
| site_id | BC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE SAM B 6735 |
| Chain | Residue |
| B | HOH659 |
| B | HOH672 |
| B | HOH716 |
| B | HOH723 |
| Q | LYS310 |
| B | VAL72 |
| B | ALA73 |
| B | GLY74 |
| B | TYR75 |
| B | ALA222 |
| B | TYR223 |
| B | ASP248 |
| B | ILE249 |
| B | LEU250 |
| B | ASN251 |
| B | HIS252 |
| B | TYR285 |
| B | TYR297 |
| B | PHE299 |
| B | EDO477 |
| B | HOH544 |
| B | HOH555 |
| B | HOH604 |
| B | HOH646 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 474 |
| Chain | Residue |
| B | VAL300 |
| B | TYR444 |
| B | GLN452 |
| B | HOH581 |
| B | HOH649 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 475 |
| Chain | Residue |
| B | GLY170 |
| B | THR171 |
| B | GLY172 |
| B | GLU175 |
| B | GLN314 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 476 |
| Chain | Residue |
| B | LEU424 |
| B | TYR427 |
| B | ALA428 |
| B | THR429 |
| B | HOH622 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 477 |
| Chain | Residue |
| A | ASN440 |
| A | GLU442 |
| A | EDO481 |
| B | HOH63 |
| B | VAL72 |
| B | TRP449 |
| B | HOH604 |
| B | HOH623 |
| B | SAM6735 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 478 |
| Chain | Residue |
| B | SER120 |
| B | ASN183 |
| B | GLU187 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 479 |
| Chain | Residue |
| B | GLU154 |
| B | TRP159 |
| B | TRP449 |
| B | ARG450 |
| B | GLN453 |
| B | HOH610 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine; by SETD6; alternate => ECO:0000250|UniProtKB:Q04207 |
| Chain | Residue | Details |
| P | LYS310 | |
| B | LEU146 | |
| B | ALA247 | |
| B | ASP248 | |
| B | LEU250 | |
| B | ILE275 | |
| B | GLY286 | |
| B | ALA321 | |
| Q | LYS310 | |
| A | ALA247 | |
| A | ASP248 | |
| A | LEU250 | |
| A | ILE275 | |
| A | GLY286 | |
| A | ALA321 | |
| B | LEU97 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKC/PRKCZ => ECO:0000250|UniProtKB:Q04207 |
| Chain | Residue | Details |
| P | SER311 | |
| Q | SER311 | |
| B | LYS39 | |
| B | PHE203 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methylated lysine; by autocatalysis => ECO:0000305|PubMed:30189201 |
| Chain | Residue | Details |
| A | GLU396 | |
| B | GLU396 |
