5TRL
Crystal structure of human GCN5 histone acetyltransferase domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004402 | molecular_function | histone acetyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0004402 | molecular_function | histone acetyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| C | 0004402 | molecular_function | histone acetyltransferase activity |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0004402 | molecular_function | histone acetyltransferase activity |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| E | 0004402 | molecular_function | histone acetyltransferase activity |
| E | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| F | 0004402 | molecular_function | histone acetyltransferase activity |
| F | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| G | 0004402 | molecular_function | histone acetyltransferase activity |
| G | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| H | 0004402 | molecular_function | histone acetyltransferase activity |
| H | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue SCA C 701 |
| Chain | Residue |
| C | GLN530 |
| C | LYS588 |
| C | GLY589 |
| C | TYR590 |
| C | GLY591 |
| C | THR592 |
| C | TYR613 |
| C | TYR617 |
| C | GLY620 |
| C | TYR621 |
| C | PHE622 |
| C | LEU531 |
| C | LYS624 |
| C | TYR645 |
| C | HOH804 |
| C | HOH811 |
| C | HOH818 |
| C | HOH826 |
| C | MET534 |
| C | VAL577 |
| C | CYS579 |
| C | ALA580 |
| C | VAL581 |
| C | GLN586 |
| C | VAL587 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | binding site for residue SCA D 701 |
| Chain | Residue |
| D | GLN530 |
| D | LEU531 |
| D | MET534 |
| D | VAL577 |
| D | CYS579 |
| D | ALA580 |
| D | VAL581 |
| D | GLN586 |
| D | VAL587 |
| D | LYS588 |
| D | GLY589 |
| D | GLY591 |
| D | THR592 |
| D | TYR613 |
| D | GLY620 |
| D | TYR621 |
| D | PHE622 |
| D | LYS624 |
| D | HOH808 |
| D | HOH809 |
| D | HOH814 |
| D | HOH817 |
| D | HOH819 |
| D | HOH822 |
| D | HOH824 |
| D | HOH825 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue SCA E 701 |
| Chain | Residue |
| E | GLN530 |
| E | ILE576 |
| E | VAL577 |
| E | PHE578 |
| E | CYS579 |
| E | ALA580 |
| E | VAL581 |
| E | GLN586 |
| E | VAL587 |
| E | LYS588 |
| E | GLY589 |
| E | GLY591 |
| E | THR592 |
| E | TYR613 |
| E | ALA614 |
| E | ASP615 |
| E | TYR617 |
| E | ALA618 |
| E | GLY620 |
| E | TYR621 |
| E | PHE622 |
| E | LYS624 |
| E | HOH807 |
| E | HOH821 |
| F | ARG533 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | binding site for residue SCA F 701 |
| Chain | Residue |
| F | HOH806 |
| F | HOH807 |
| F | HOH809 |
| F | HOH825 |
| F | HOH841 |
| E | ARG533 |
| E | GLU616 |
| F | GLN530 |
| F | LEU531 |
| F | VAL577 |
| F | PHE578 |
| F | CYS579 |
| F | ALA580 |
| F | VAL581 |
| F | GLN586 |
| F | VAL587 |
| F | LYS588 |
| F | GLY589 |
| F | GLY591 |
| F | THR592 |
| F | TYR613 |
| F | TYR617 |
| F | ALA618 |
| F | GLY620 |
| F | TYR621 |
| F | LYS624 |
| F | TYR645 |
| F | HOH805 |
| site_id | AC5 |
| Number of Residues | 28 |
| Details | binding site for residue SCA B 701 |
| Chain | Residue |
| A | ARG533 |
| A | TYR617 |
| B | GLN530 |
| B | LEU531 |
| B | VAL577 |
| B | PHE578 |
| B | CYS579 |
| B | ALA580 |
| B | VAL581 |
| B | GLN586 |
| B | VAL587 |
| B | LYS588 |
| B | GLY589 |
| B | TYR590 |
| B | GLY591 |
| B | THR592 |
| B | TYR613 |
| B | ALA614 |
| B | ASP615 |
| B | TYR617 |
| B | ALA618 |
| B | GLY620 |
| B | TYR621 |
| B | LYS624 |
| B | HOH802 |
| B | HOH806 |
| B | HOH809 |
| B | HOH815 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | binding site for residue SCA A 701 |
| Chain | Residue |
| A | LEU531 |
| A | VAL577 |
| A | PHE578 |
| A | CYS579 |
| A | ALA580 |
| A | VAL581 |
| A | GLN586 |
| A | VAL587 |
| A | LYS588 |
| A | GLY589 |
| A | GLY591 |
| A | THR592 |
| A | TYR613 |
| A | ALA614 |
| A | ASP615 |
| A | TYR617 |
| A | ALA618 |
| A | GLY620 |
| A | TYR621 |
| A | LYS624 |
| A | HOH805 |
| A | HOH843 |
| A | HOH845 |
| B | ARG533 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | binding site for residue SCA G 701 |
| Chain | Residue |
| G | LEU531 |
| G | VAL577 |
| G | CYS579 |
| G | ALA580 |
| G | VAL581 |
| G | GLN586 |
| G | VAL587 |
| G | LYS588 |
| G | GLY589 |
| G | TYR590 |
| G | GLY591 |
| G | THR592 |
| G | TYR613 |
| G | TYR617 |
| G | ALA618 |
| G | GLY620 |
| G | TYR621 |
| G | PHE622 |
| G | LYS624 |
| G | HOH803 |
| G | HOH810 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | binding site for residue SCA H 701 |
| Chain | Residue |
| H | MET534 |
| H | VAL577 |
| H | PHE578 |
| H | CYS579 |
| H | ALA580 |
| H | VAL581 |
| H | GLN586 |
| H | VAL587 |
| H | LYS588 |
| H | GLY589 |
| H | TYR590 |
| H | GLY591 |
| H | THR592 |
| H | TYR613 |
| H | TYR617 |
| H | ALA618 |
| H | TYR621 |
| H | PHE622 |
| H | LYS624 |
| H | TYR645 |
| H | HOH801 |
| H | HOH807 |
| H | HOH813 |
| H | HOH830 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:31527837 |
| Chain | Residue | Details |
| C | GLU575 | |
| D | GLU575 | |
| E | GLU575 | |
| F | GLU575 | |
| B | GLU575 | |
| A | GLU575 | |
| G | GLU575 | |
| H | GLU575 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29211711, ECO:0007744|PDB:5TRL |
| Chain | Residue | Details |
| C | CYS579 | |
| F | CYS579 | |
| F | GLN586 | |
| F | TYR617 | |
| B | CYS579 | |
| B | GLN586 | |
| B | TYR617 | |
| A | CYS579 | |
| A | GLN586 | |
| A | TYR617 | |
| G | CYS579 | |
| C | GLN586 | |
| G | GLN586 | |
| G | TYR617 | |
| H | CYS579 | |
| H | GLN586 | |
| H | TYR617 | |
| C | TYR617 | |
| D | CYS579 | |
| D | GLN586 | |
| D | TYR617 | |
| E | CYS579 | |
| E | GLN586 | |
| E | TYR617 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:23142079 |
| Chain | Residue | Details |
| C | LYS549 | |
| D | LYS549 | |
| E | LYS549 | |
| F | LYS549 | |
| B | LYS549 | |
| A | LYS549 | |
| G | LYS549 | |
| H | LYS549 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 524 |
| Chain | Residue | Details |
| C | PHE568 | electrostatic stabiliser |
| C | PHE573 | electrostatic stabiliser |
| C | GLU575 | proton acceptor |
| C | ILE576 | electrostatic stabiliser |
| C | VAL577 | electrostatic stabiliser |
| C | CYS579 | electrostatic stabiliser |
| C | LEU611 | electrostatic stabiliser |
| C | ILE642 | electrostatic stabiliser |
| C | TYR645 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 524 |
| Chain | Residue | Details |
| D | PHE568 | electrostatic stabiliser |
| D | PHE573 | electrostatic stabiliser |
| D | GLU575 | proton acceptor |
| D | ILE576 | electrostatic stabiliser |
| D | VAL577 | electrostatic stabiliser |
| D | CYS579 | electrostatic stabiliser |
| D | LEU611 | electrostatic stabiliser |
| D | ILE642 | electrostatic stabiliser |
| D | TYR645 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 9 |
| Details | M-CSA 524 |
| Chain | Residue | Details |
| E | PHE568 | electrostatic stabiliser |
| E | PHE573 | electrostatic stabiliser |
| E | GLU575 | proton acceptor |
| E | ILE576 | electrostatic stabiliser |
| E | VAL577 | electrostatic stabiliser |
| E | CYS579 | electrostatic stabiliser |
| E | LEU611 | electrostatic stabiliser |
| E | ILE642 | electrostatic stabiliser |
| E | TYR645 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 9 |
| Details | M-CSA 524 |
| Chain | Residue | Details |
| F | PHE568 | electrostatic stabiliser |
| F | PHE573 | electrostatic stabiliser |
| F | GLU575 | proton acceptor |
| F | ILE576 | electrostatic stabiliser |
| F | VAL577 | electrostatic stabiliser |
| F | CYS579 | electrostatic stabiliser |
| F | LEU611 | electrostatic stabiliser |
| F | ILE642 | electrostatic stabiliser |
| F | TYR645 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 9 |
| Details | M-CSA 524 |
| Chain | Residue | Details |
| B | PHE568 | electrostatic stabiliser |
| B | PHE573 | electrostatic stabiliser |
| B | GLU575 | proton acceptor |
| B | ILE576 | electrostatic stabiliser |
| B | VAL577 | electrostatic stabiliser |
| B | CYS579 | electrostatic stabiliser |
| B | LEU611 | electrostatic stabiliser |
| B | ILE642 | electrostatic stabiliser |
| B | TYR645 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 9 |
| Details | M-CSA 524 |
| Chain | Residue | Details |
| A | PHE568 | electrostatic stabiliser |
| A | PHE573 | electrostatic stabiliser |
| A | GLU575 | proton acceptor |
| A | ILE576 | electrostatic stabiliser |
| A | VAL577 | electrostatic stabiliser |
| A | CYS579 | electrostatic stabiliser |
| A | LEU611 | electrostatic stabiliser |
| A | ILE642 | electrostatic stabiliser |
| A | TYR645 | electrostatic stabiliser |
| site_id | MCSA7 |
| Number of Residues | 9 |
| Details | M-CSA 524 |
| Chain | Residue | Details |
| G | PHE568 | electrostatic stabiliser |
| G | PHE573 | electrostatic stabiliser |
| G | GLU575 | proton acceptor |
| G | ILE576 | electrostatic stabiliser |
| G | VAL577 | electrostatic stabiliser |
| G | CYS579 | electrostatic stabiliser |
| G | LEU611 | electrostatic stabiliser |
| G | ILE642 | electrostatic stabiliser |
| G | TYR645 | electrostatic stabiliser |
| site_id | MCSA8 |
| Number of Residues | 9 |
| Details | M-CSA 524 |
| Chain | Residue | Details |
| H | PHE568 | electrostatic stabiliser |
| H | PHE573 | electrostatic stabiliser |
| H | GLU575 | proton acceptor |
| H | ILE576 | electrostatic stabiliser |
| H | VAL577 | electrostatic stabiliser |
| H | CYS579 | electrostatic stabiliser |
| H | LEU611 | electrostatic stabiliser |
| H | ILE642 | electrostatic stabiliser |
| H | TYR645 | electrostatic stabiliser |
