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 | protein-N-terminal amino-acid acetyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0004596 | molecular_function | protein-N-terminal amino-acid acetyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| C | 0004596 | molecular_function | protein-N-terminal amino-acid acetyltransferase activity |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0004596 | molecular_function | protein-N-terminal amino-acid 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 | 338 |
| Details | Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Region: {"description":"Required for homodimerization","evidences":[{"source":"PubMed","id":"27320834","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"27320834","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27550639","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27320834","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ICV","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5ICW","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 44 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27320834","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27550639","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5HGZ","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5HH0","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5HH1","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5ICV","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5ICW","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Required to position thioacetyl group","evidences":[{"source":"PubMed","id":"27550639","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"21981917","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"21981917","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
