4XNH
Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a bisubstrate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0031415 | cellular_component | NatA complex |
A | 0043022 | molecular_function | ribosome binding |
B | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006474 | biological_process | N-terminal protein amino acid acetylation |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0031415 | cellular_component | NatA complex |
B | 0042802 | molecular_function | identical protein binding |
B | 1990189 | molecular_function | peptide-serine-alpha-N-acetyltransferase activity |
B | 1990190 | molecular_function | peptide-glutamate-alpha-N-acetyltransferase activity |
C | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0007064 | biological_process | mitotic sister chromatid cohesion |
C | 0016746 | molecular_function | acyltransferase activity |
C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
C | 0031415 | cellular_component | NatA complex |
C | 0120518 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | binding site for residue IHP A 901 |
Chain | Residue |
A | LYS349 |
A | HOH1002 |
A | HOH1031 |
A | HOH1093 |
A | HOH1128 |
A | HOH1214 |
A | HOH1221 |
A | HOH1290 |
A | HOH1333 |
B | LYS80 |
B | TYR85 |
A | ILE422 |
B | LYS91 |
B | THR123 |
B | TYR124 |
A | ARG426 |
A | LYS429 |
A | HIS430 |
A | LYS457 |
A | LYS460 |
A | TYR461 |
A | ARG464 |
site_id | AC2 |
Number of Residues | 27 |
Details | binding site for residue ACO C 201 |
Chain | Residue |
A | GLN320 |
A | HOH1037 |
A | HOH1091 |
C | THR26 |
C | TYR31 |
C | ILE93 |
C | GLU94 |
C | PHE95 |
C | LEU96 |
C | GLY97 |
C | VAL98 |
C | ARG103 |
C | HIS104 |
C | LYS105 |
C | SER106 |
C | ILE107 |
C | GLY108 |
C | SER109 |
C | TYR130 |
C | TRP141 |
C | HOH301 |
C | HOH316 |
C | HOH320 |
C | HOH321 |
C | HOH322 |
C | HOH323 |
C | HOH324 |
site_id | AC3 |
Number of Residues | 32 |
Details | binding site for residue CMC F 301 |
Chain | Residue |
B | ASN23 |
B | LEU24 |
B | SER117 |
B | LEU118 |
B | SER119 |
B | VAL120 |
B | ARG125 |
B | ARG126 |
B | MET127 |
B | GLY128 |
B | ILE129 |
B | ALA130 |
B | GLU131 |
B | HIS153 |
B | VAL154 |
B | ASN158 |
B | ALA160 |
B | HIS163 |
B | TYR165 |
B | THR168 |
B | ARG207 |
B | HOH305 |
B | HOH326 |
C | GLU68 |
F | SER1 |
F | HOH401 |
F | HOH404 |
F | HOH405 |
F | HOH406 |
F | HOH407 |
F | HOH408 |
F | HOH411 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine; in Corticotropin => ECO:0000250|UniProtKB:P01191 |
Chain | Residue | Details |
F | SER1 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | SER674 |