5ICW
Crystal structure of human NatF (hNaa60) homodimer bound to Coenzyme A
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 |
| C | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue COA A 201 |
| Chain | Residue |
| A | LEU101 |
| A | ASN143 |
| A | THR145 |
| A | PHE149 |
| A | ASN152 |
| A | ARG153 |
| A | HOH319 |
| A | HOH322 |
| A | HOH331 |
| A | HOH334 |
| A | HOH337 |
| A | GLY102 |
| A | HOH353 |
| A | HOH375 |
| A | HOH385 |
| A | HOH389 |
| C | LYS76 |
| A | VAL103 |
| A | ARG108 |
| A | LYS109 |
| A | HIS110 |
| A | GLY111 |
| A | GLY113 |
| A | SER114 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 202 |
| Chain | Residue |
| A | VAL139 |
| A | LEU140 |
| A | ASN143 |
| A | HOH342 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue COA B 201 |
| Chain | Residue |
| B | PHE34 |
| B | LEU101 |
| B | GLY102 |
| B | VAL103 |
| B | ARG108 |
| B | LYS109 |
| B | HIS110 |
| B | GLY111 |
| B | GLY113 |
| B | SER114 |
| B | ASN143 |
| B | THR145 |
| B | PHE149 |
| B | TYR150 |
| B | ASN152 |
| B | ARG153 |
| B | HOH305 |
| B | HOH320 |
| B | HOH322 |
| B | HOH328 |
| B | HOH334 |
| B | HOH348 |
| B | HOH361 |
| B | HOH366 |
| B | HOH372 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 202 |
| Chain | Residue |
| A | ILE167 |
| B | VAL139 |
| B | LEU140 |
| B | ASN143 |
| B | HOH348 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | binding site for residue COA C 201 |
| Chain | Residue |
| A | ASN73 |
| C | PHE34 |
| C | LEU101 |
| C | GLY102 |
| C | VAL103 |
| C | ARG108 |
| C | LYS109 |
| C | HIS110 |
| C | GLY111 |
| C | GLY113 |
| C | SER114 |
| C | ASN143 |
| C | THR145 |
| C | PHE149 |
| C | ASN152 |
| C | ARG153 |
| C | CL202 |
| C | HOH306 |
| C | HOH316 |
| C | HOH318 |
| C | HOH320 |
| C | HOH334 |
| C | HOH344 |
| C | HOH356 |
| C | HOH357 |
| C | HOH399 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 202 |
| Chain | Residue |
| C | LEU140 |
| C | ASN143 |
| C | COA201 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | binding site for residue COA D 201 |
| Chain | Residue |
| D | SER114 |
| D | ASN143 |
| D | THR145 |
| D | ALA146 |
| D | PHE149 |
| D | TYR150 |
| D | ASN152 |
| D | ARG153 |
| D | HOH315 |
| D | HOH316 |
| D | HOH318 |
| D | HOH324 |
| D | HOH367 |
| B | ASN73 |
| B | HOH340 |
| D | PHE34 |
| D | LEU101 |
| D | GLY102 |
| D | VAL103 |
| D | ARG108 |
| D | LYS109 |
| D | HIS110 |
| D | GLY111 |
| D | ILE112 |
| D | GLY113 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 202 |
| Chain | Residue |
| D | LEU140 |
| D | ASN143 |
| D | HOH369 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:27320834, ECO:0000269|PubMed:27550639 |
| Chain | Residue | Details |
| A | TYR97 | |
| A | HIS138 | |
| B | TYR97 | |
| B | HIS138 | |
| C | TYR97 | |
| C | HIS138 | |
| D | TYR97 | |
| D | HIS138 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27320834, ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW |
| Chain | Residue | Details |
| A | TYR38 | |
| D | TYR38 | |
| D | LEU99 | |
| D | TYR165 | |
| A | LEU99 | |
| A | TYR165 | |
| B | TYR38 | |
| B | LEU99 | |
| B | TYR165 | |
| C | TYR38 | |
| C | LEU99 | |
| C | TYR165 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| 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 | |
| C | LYS109 | |
| C | ASN143 | |
| C | TYR150 | |
| D | LEU101 | |
| D | LYS109 | |
| D | ASN143 | |
| D | TYR150 | |
| A | LYS109 | |
| A | ASN143 | |
| A | TYR150 | |
| B | LEU101 | |
| B | LYS109 | |
| B | ASN143 | |
| B | TYR150 | |
| C | LEU101 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Required to position thioacetyl group => ECO:0000269|PubMed:27550639 |
| Chain | Residue | Details |
| A | PHE34 | |
| B | PHE34 | |
| C | PHE34 | |
| D | PHE34 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:21981917 |
| Chain | Residue | Details |
| A | LYS79 | |
| D | LYS79 | |
| D | LYS105 | |
| D | LYS156 | |
| A | LYS105 | |
| A | LYS156 | |
| B | LYS79 | |
| B | LYS105 | |
| B | LYS156 | |
| C | LYS79 | |
| C | LYS105 | |
| C | LYS156 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000305|PubMed:21981917 |
| Chain | Residue | Details |
| A | LYS109 | |
| A | LYS121 | |
| B | LYS109 | |
| B | LYS121 | |
| C | LYS109 | |
| C | LYS121 | |
| D | LYS109 | |
| D | LYS121 |
