5ICV
Crystal structure of human NatF (hNaa60) bound to a bisubstrate analogue
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 36 |
Details | binding site for Di-peptide 1XE C 101 and MET C 1 |
Chain | Residue |
A | PHE34 |
A | HIS110 |
A | GLY111 |
A | ILE112 |
A | GLY113 |
A | SER114 |
A | HIS138 |
A | ASN143 |
A | THR145 |
A | PHE149 |
A | TYR150 |
A | ILE36 |
A | ASN152 |
A | ARG153 |
A | TYR165 |
A | HOH222 |
A | HOH223 |
A | HOH224 |
A | HOH267 |
B | ASN152 |
B | ARG153 |
C | LYS2 |
A | LEU99 |
C | ALA3 |
C | HOH201 |
C | HOH202 |
C | HOH203 |
C | HOH205 |
D | 1XE101 |
D | HOH206 |
A | SER100 |
A | LEU101 |
A | GLY102 |
A | VAL103 |
A | ARG108 |
A | LYS109 |
site_id | AC2 |
Number of Residues | 36 |
Details | binding site for Di-peptide 1XE D 101 and MET D 1 |
Chain | Residue |
A | ASN152 |
A | ARG153 |
B | PHE34 |
B | ILE36 |
B | LEU99 |
B | SER100 |
B | LEU101 |
B | GLY102 |
B | VAL103 |
B | ARG108 |
B | LYS109 |
B | HIS110 |
B | GLY111 |
B | ILE112 |
B | GLY113 |
B | SER114 |
B | HIS138 |
B | ASN143 |
B | THR145 |
B | PHE149 |
B | TYR150 |
B | ASN152 |
B | ARG153 |
B | TYR165 |
B | HOH237 |
B | HOH259 |
C | 1XE101 |
D | LYS2 |
D | ALA3 |
D | HOH201 |
D | HOH203 |
D | HOH204 |
D | HOH205 |
D | HOH206 |
D | HOH207 |
D | HOH208 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:27320834, ECO:0000269|PubMed:27550639 |
Chain | Residue | Details |
A | TYR97 | |
A | HIS138 | |
B | TYR97 | |
B | HIS138 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27320834, ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW |
Chain | Residue | Details |
A | TYR38 | |
A | LEU99 | |
A | TYR165 | |
B | TYR38 | |
B | LEU99 | |
B | TYR165 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27320834, ECO:0000269|PubMed:27550639, ECO:0000312|PDB:5HGZ, ECO:0000312|PDB:5HH0, ECO:0000312|PDB:5HH1, ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW |
Chain | Residue | Details |
A | LEU101 | |
A | LYS109 | |
A | ASN143 | |
A | TYR150 | |
B | LEU101 | |
B | LYS109 | |
B | ASN143 | |
B | TYR150 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Required to position thioacetyl group => ECO:0000269|PubMed:27550639 |
Chain | Residue | Details |
A | PHE34 | |
B | PHE34 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:21981917 |
Chain | Residue | Details |
A | LYS79 | |
A | LYS105 | |
A | LYS156 | |
B | LYS79 | |
B | LYS105 | |
B | LYS156 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000305|PubMed:21981917 |
Chain | Residue | Details |
A | LYS109 | |
A | LYS121 | |
B | LYS109 | |
B | LYS121 |