6PDA
Crystal structure of MYST acetyltransferase domain in complex with inhibitor 74
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 801 |
Chain | Residue |
A | CYS540 |
A | CYS543 |
A | HIS556 |
A | CYS560 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue NA A 802 |
Chain | Residue |
A | ASP520 |
A | HOH913 |
A | HOH932 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL A 803 |
Chain | Residue |
A | SER693 |
A | O9J806 |
A | ARG655 |
A | SER690 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue GOL A 804 |
Chain | Residue |
A | LYS573 |
A | GLN731 |
A | VAL736 |
A | HIS743 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 805 |
Chain | Residue |
A | TYR517 |
A | ARG656 |
site_id | AC6 |
Number of Residues | 16 |
Details | binding site for residue O9J A 806 |
Chain | Residue |
A | PHE600 |
A | LEU601 |
A | ILE649 |
A | GLN654 |
A | ARG655 |
A | ARG656 |
A | GLY657 |
A | TYR658 |
A | GLY659 |
A | ARG660 |
A | SER684 |
A | LEU686 |
A | SER690 |
A | SER693 |
A | GOL803 |
A | HOH931 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 25 |
Details | ZN_FING: C2HC MYST-type => ECO:0000255|PROSITE-ProRule:PRU01063, ECO:0000269|PubMed:22020126 |
Chain | Residue | Details |
A | LEU537-TRP562 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:21217699, ECO:0000305|PubMed:27768893, ECO:0000305|PubMed:33657400 |
Chain | Residue | Details |
A | GLU680 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:21691301, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:27382063, ECO:0000269|PubMed:29321206, ECO:0000269|Ref.33, ECO:0007744|PDB:2GIV, ECO:0007744|PDB:2PQ8, ECO:0007744|PDB:2Y0M, ECO:0007744|PDB:3QAH, ECO:0007744|PDB:3TOA, ECO:0007744|PDB:3TOB, ECO:0007744|PDB:4DNC, ECO:0007744|PDB:5J8C, ECO:0007744|PDB:5J8F, ECO:0007744|PDB:5WCI |
Chain | Residue | Details |
A | CYS540 | |
A | CYS543 | |
A | HIS556 | |
A | CYS560 |
site_id | SWS_FT_FI4 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29321206, ECO:0007744|PDB:5WCI |
Chain | Residue | Details |
A | ILE647 | |
A | ILE649 | |
A | ARG655 | |
A | GLY659 | |
A | ARG660 | |
A | SER684 | |
A | SER693 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.33, ECO:0007744|PDB:2GIV, ECO:0007744|PDB:2Y0M |
Chain | Residue | Details |
A | ARG656 | |
A | GLY657 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0007744|PDB:2Y0M |
Chain | Residue | Details |
A | TYR738 | |
A | LYS762 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:21691301, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22547026, ECO:0000269|PubMed:22918831, ECO:0000269|PubMed:27382063, ECO:0000269|Ref.33, ECO:0007744|PDB:2GIV |
Chain | Residue | Details |
A | ALY604 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER678 |