4U9W
Crystal Structure of NatD bound to H4/H2A peptide and CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010485 | molecular_function | histone H4 acetyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0043998 | molecular_function | histone H2A acetyltransferase activity |
| B | 0010485 | molecular_function | histone H4 acetyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0043998 | molecular_function | histone H2A acetyltransferase activity |
| C | 0010485 | molecular_function | histone H4 acetyltransferase activity |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| C | 0043998 | molecular_function | histone H2A acetyltransferase activity |
| D | 0010485 | molecular_function | histone H4 acetyltransferase activity |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0043998 | molecular_function | histone H2A acetyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue COA A 301 |
| Chain | Residue |
| A | VAL140 |
| A | ASN179 |
| A | GLY181 |
| A | ALA182 |
| A | GLN184 |
| A | PHE185 |
| A | ALA189 |
| A | NA302 |
| A | HOH438 |
| A | HOH454 |
| A | HOH486 |
| A | GLN141 |
| D | GOL302 |
| F | SER1 |
| A | LEU142 |
| A | ARG147 |
| A | ARG148 |
| A | LYS149 |
| A | GLY150 |
| A | GLY152 |
| A | LYS153 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 302 |
| Chain | Residue |
| A | GLU139 |
| A | VAL140 |
| A | GLN141 |
| A | COA301 |
| F | SER1 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | TYR85 |
| A | TRP90 |
| A | LYS97 |
| A | GLU100 |
| B | GLY14 |
| F | GLY2 |
| F | ARG3 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 304 |
| Chain | Residue |
| A | GLN157 |
| A | GLN160 |
| A | HOH472 |
| A | HOH505 |
| B | GLN160 |
| B | ASN164 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | binding site for residue COA B 301 |
| Chain | Residue |
| B | VAL140 |
| B | GLN141 |
| B | LEU142 |
| B | ARG147 |
| B | ARG148 |
| B | LYS149 |
| B | GLY150 |
| B | GLY152 |
| B | LYS153 |
| B | ASN179 |
| B | GLY181 |
| B | GLN184 |
| B | PHE185 |
| B | ALA189 |
| B | HOH430 |
| B | HOH435 |
| B | HOH436 |
| B | HOH502 |
| B | HOH507 |
| E | SER1 |
| E | NA101 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | binding site for residue COA C 301 |
| Chain | Residue |
| C | VAL140 |
| C | GLN141 |
| C | LEU142 |
| C | ARG147 |
| C | ARG148 |
| C | LYS149 |
| C | GLY150 |
| C | LEU151 |
| C | GLY152 |
| C | LYS153 |
| C | ASN179 |
| C | GLY181 |
| C | GLN184 |
| C | PHE185 |
| C | PHE186 |
| C | ALA189 |
| C | NA302 |
| C | HOH414 |
| C | HOH421 |
| C | HOH431 |
| C | HOH443 |
| G | SER1 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NA C 302 |
| Chain | Residue |
| C | GLU139 |
| C | VAL140 |
| C | GLN141 |
| C | COA301 |
| G | SER1 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 303 |
| Chain | Residue |
| C | TYR85 |
| C | TRP90 |
| C | LYS97 |
| C | GLU100 |
| G | GLY2 |
| G | ARG3 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | binding site for residue COA D 301 |
| Chain | Residue |
| D | GLY150 |
| D | GLY152 |
| D | LYS153 |
| D | ASN179 |
| D | GLY181 |
| D | GLN184 |
| D | PHE185 |
| D | ALA189 |
| D | HOH413 |
| D | HOH420 |
| D | HOH423 |
| D | HOH435 |
| D | HOH441 |
| H | SER1 |
| H | NA101 |
| D | VAL140 |
| D | GLN141 |
| D | LEU142 |
| D | ARG147 |
| D | ARG148 |
| D | LYS149 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 302 |
| Chain | Residue |
| A | GLN184 |
| A | GLU188 |
| A | COA301 |
| D | ILE194 |
| D | SER200 |
| D | MET201 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue NA E 101 |
| Chain | Residue |
| B | GLU139 |
| B | VAL140 |
| B | COA301 |
| E | SER1 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue NA H 101 |
| Chain | Residue |
| D | GLU139 |
| D | VAL140 |
| D | COA301 |
| H | SER1 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25619998","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4U9W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25619998","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4U9V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4U9W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Essential for catalytic activity","evidences":[{"source":"PubMed","id":"25619998","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17967882","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate","evidences":[{"source":"UniProtKB","id":"P62806","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-lactoyllysine; alternate","evidences":[{"source":"PubMed","id":"31645732","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
