4UA3
Crystal structure of selenomethionine labeled SpNatD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0010485 | molecular_function | histone H4 acetyltransferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0032153 | cellular_component | cell division site |
| A | 0043998 | molecular_function | histone H2A acetyltransferase activity |
| A | 0051604 | biological_process | protein maturation |
| A | 1990189 | molecular_function | peptide-serine-alpha-N-acetyltransferase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006338 | biological_process | chromatin remodeling |
| B | 0010485 | molecular_function | histone H4 acetyltransferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0032153 | cellular_component | cell division site |
| B | 0043998 | molecular_function | histone H2A acetyltransferase activity |
| B | 0051604 | biological_process | protein maturation |
| B | 1990189 | molecular_function | peptide-serine-alpha-N-acetyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue COA A 301 |
| Chain | Residue |
| A | ILE120 |
| A | LYS133 |
| A | ASN159 |
| A | ASN161 |
| A | ASN164 |
| A | PHE165 |
| A | TYR166 |
| A | HIS168 |
| A | PHE169 |
| A | CL302 |
| A | HOH470 |
| A | GLN121 |
| A | HOH476 |
| A | HOH524 |
| B | ARG13 |
| B | LEU160 |
| B | ASN164 |
| B | COA301 |
| A | LEU122 |
| A | ARG127 |
| A | GLY128 |
| A | ARG129 |
| A | ASN130 |
| A | VAL131 |
| A | GLY132 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | VAL155 |
| A | PHE156 |
| A | ASN159 |
| A | COA301 |
| B | ARG13 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | binding site for residue COA B 301 |
| Chain | Residue |
| A | ARG13 |
| A | LEU160 |
| A | ASN161 |
| A | ASN164 |
| A | COA301 |
| B | ILE120 |
| B | GLN121 |
| B | LEU122 |
| B | ARG127 |
| B | GLY128 |
| B | ARG129 |
| B | ASN130 |
| B | VAL131 |
| B | GLY132 |
| B | LYS133 |
| B | ASN159 |
| B | ASN161 |
| B | ALA162 |
| B | ASN164 |
| B | PHE165 |
| B | TYR166 |
| B | HIS168 |
| B | PHE169 |
| B | HOH449 |
| B | HOH453 |
| B | HOH456 |
| B | HOH468 |
| B | HOH481 |
| B | HOH498 |
| B | HOH509 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q86UY6 |
| Chain | Residue | Details |
| A | TYR64 | |
| B | SER176 | |
| A | THR107 | |
| A | TYR118 | |
| A | THR154 | |
| A | SER176 | |
| B | TYR64 | |
| B | THR107 | |
| B | TYR118 | |
| B | THR154 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25619998, ECO:0000312|PDB:4UA3 |
| Chain | Residue | Details |
| A | ILE120 | |
| A | GLY128 | |
| A | ASN159 | |
| B | ILE120 | |
| B | GLY128 | |
| B | ASN159 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Essential for catalytic activity => ECO:0000250|UniProtKB:Q86UY6 |
| Chain | Residue | Details |
| A | GLU119 | |
| B | GLU119 |
