5MU6
Human N-myristoyltransferase (NMT1) with Myristoyl-CoA and IMP-1088 inhibitor bound
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue MYA A 501 |
| Chain | Residue |
| A | TYR117 |
| A | VAL250 |
| A | ARG255 |
| A | SER256 |
| A | ARG258 |
| A | VAL259 |
| A | ALA260 |
| A | PRO261 |
| A | THR268 |
| A | PHE277 |
| A | THR282 |
| A | GLN118 |
| A | LEU287 |
| A | TYR479 |
| A | MG502 |
| A | HOH622 |
| A | HOH665 |
| A | HOH693 |
| A | HOH726 |
| A | HOH756 |
| A | HOH758 |
| A | PHE119 |
| A | TRP120 |
| A | TYR180 |
| A | VAL181 |
| A | PHE247 |
| A | LEU248 |
| A | CYS249 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | LEU254 |
| A | ARG255 |
| A | SER256 |
| A | LYS257 |
| A | ARG258 |
| A | VAL259 |
| A | MYA501 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | LYS289 |
| A | PRO290 |
| A | VAL291 |
| A | LEU478 |
| A | TRP481 |
| A | LYS482 |
| A | CYS483 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | GLU244 |
| A | TRP374 |
| A | TYR423 |
| A | VAL494 |
| A | GLN496 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue KFK A 505 |
| Chain | Residue |
| A | VAL181 |
| A | PHE188 |
| A | PHE190 |
| A | ASN246 |
| A | THR282 |
| A | TYR296 |
| A | HIS298 |
| A | SER405 |
| A | TYR420 |
| A | ASN451 |
| A | ALA452 |
| A | LEU495 |
| A | GLN496 |
| site_id | AC6 |
| Number of Residues | 31 |
| Details | binding site for residue MYA B 501 |
| Chain | Residue |
| B | ARG115 |
| B | TYR117 |
| B | GLN118 |
| B | PHE119 |
| B | TRP120 |
| B | TYR180 |
| B | VAL181 |
| B | ILE245 |
| B | PHE247 |
| B | LEU248 |
| B | CYS249 |
| B | VAL250 |
| B | ARG255 |
| B | SER256 |
| B | LYS257 |
| B | ARG258 |
| B | VAL259 |
| B | ALA260 |
| B | PRO261 |
| B | THR268 |
| B | PHE277 |
| B | ALA279 |
| B | TYR281 |
| B | THR282 |
| B | LEU287 |
| B | MG502 |
| B | HOH642 |
| B | HOH661 |
| B | HOH695 |
| B | HOH723 |
| B | HOH729 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | LEU254 |
| B | SER256 |
| B | LYS257 |
| B | ARG258 |
| B | VAL259 |
| B | MYA501 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | LEU478 |
| B | TRP481 |
| B | LYS482 |
| B | CYS483 |
| B | HOH614 |
| B | PRO126 |
| B | LYS289 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | GLU244 |
| B | TRP374 |
| B | TYR423 |
| B | VAL494 |
| B | GLN496 |
| B | HOH635 |
| site_id | AD1 |
| Number of Residues | 14 |
| Details | binding site for residue KFK B 505 |
| Chain | Residue |
| B | VAL181 |
| B | PHE188 |
| B | ARG189 |
| B | PHE190 |
| B | ASN246 |
| B | THR282 |
| B | TYR296 |
| B | HIS298 |
| B | SER405 |
| B | TYR420 |
| B | ASN451 |
| B | ALA452 |
| B | LEU495 |
| B | GLN496 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25255805","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32111831","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD90055.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25255805","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32103017","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32111831","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD90055.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32103017","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25255805","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD90055.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
