6OIP
Crystal structure of MYST acetyltransferase domain in complex with inhibitor 34
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 501 |
Chain | Residue |
A | CYS210 |
A | CYS213 |
A | HIS226 |
A | CYS230 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | HOH611 |
A | HOH624 |
A | LYS243 |
A | ILE246 |
A | GLN401 |
A | VAL406 |
A | HIS413 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | SER360 |
A | SER363 |
A | MLS504 |
site_id | AC4 |
Number of Residues | 14 |
Details | binding site for residue MLS A 504 |
Chain | Residue |
A | GLN324 |
A | ARG325 |
A | ARG326 |
A | GLY327 |
A | TYR328 |
A | GLY329 |
A | ARG330 |
A | LEU356 |
A | SER360 |
A | SER363 |
A | TYR364 |
A | GLN430 |
A | GOL503 |
A | HOH649 |
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 | LEU207-TRP232 |
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 | GLU350 |
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 | CYS210 | |
A | CYS213 | |
A | HIS226 | |
A | CYS230 |
site_id | SWS_FT_FI4 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29321206, ECO:0007744|PDB:5WCI |
Chain | Residue | Details |
A | ILE317 | |
A | ILE319 | |
A | ARG325 | |
A | GLY329 | |
A | ARG330 | |
A | SER354 | |
A | SER363 |
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 | ARG326 | |
A | GLY327 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0007744|PDB:2Y0M |
Chain | Residue | Details |
A | TYR408 | |
A | LYS432 |
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 | ALY274 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER348 |