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 | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:17967882 |
Chain | Residue | Details |
E | SER1 | |
B | THR174 | |
B | SER197 | |
B | TYR211 | |
C | TYR85 | |
C | ASP127 | |
C | TYR138 | |
C | THR174 | |
C | SER197 | |
C | TYR211 | |
D | TYR85 | |
F | SER1 | |
D | ASP127 | |
D | TYR138 | |
D | THR174 | |
D | SER197 | |
D | TYR211 | |
G | SER1 | |
H | SER1 | |
A | SER197 | |
A | TYR211 | |
B | TYR85 | |
B | ASP127 | |
B | TYR138 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62806 |
Chain | Residue | Details |
E | ARG3 | |
D | VAL140 | |
D | ARG148 | |
D | ASN179 | |
F | ARG3 | |
G | ARG3 | |
H | ARG3 | |
B | ARG148 | |
B | ASN179 | |
C | VAL140 | |
C | ARG148 | |
C | ASN179 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 |
Chain | Residue | Details |
E | LYS5 | |
F | LYS5 | |
G | LYS5 | |
H | LYS5 |