6SK8
DeltaC3 C-terminal truncation of HsNMT1 in complex with MyrCoA and GDCFSKPR substrates
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | binding site for residue MYA A 501 |
| Chain | Residue |
| A | ARG115 |
| A | CYS249 |
| A | VAL250 |
| A | ARG255 |
| A | SER256 |
| A | LYS257 |
| A | ARG258 |
| A | VAL259 |
| A | ALA260 |
| A | PRO261 |
| A | THR268 |
| A | TYR117 |
| A | VAL271 |
| A | PHE277 |
| A | GLN278 |
| A | TYR281 |
| A | THR282 |
| A | LEU287 |
| A | TYR479 |
| A | HOH623 |
| A | HOH657 |
| A | HOH692 |
| A | GLN118 |
| A | HOH724 |
| A | HOH752 |
| A | HOH755 |
| A | HOH814 |
| A | HOH815 |
| A | PHE119 |
| A | TRP120 |
| A | ASN179 |
| A | TYR180 |
| A | PHE247 |
| A | LEU248 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | LYS305 |
| A | HIS413 |
| A | LYS414 |
| A | SER415 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | HIS426 |
| A | THR427 |
| A | GLN428 |
| A | THR429 |
| A | PRO430 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | PRO126 |
| A | LYS289 |
| A | VAL291 |
| A | LEU478 |
| A | TRP481 |
| A | LYS482 |
| A | CYS483 |
| A | HOH702 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | LEU161 |
| A | LEU163 |
| A | ARG202 |
| A | TRP206 |
| A | HIS211 |
| A | HOH906 |
| site_id | AC6 |
| Number of Residues | 33 |
| Details | binding site for residue MYA B 501 |
| Chain | Residue |
| B | ARG115 |
| B | TYR117 |
| B | GLN118 |
| B | PHE119 |
| B | TRP120 |
| B | ASN179 |
| B | TYR180 |
| B | VAL181 |
| B | ASN246 |
| 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 | TYR479 |
| B | HOH627 |
| B | HOH649 |
| B | HOH669 |
| B | HOH677 |
| B | HOH809 |
| B | HOH820 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | HOH717 |
| A | GLY275 |
| B | ASN232 |
| B | VAL365 |
| B | MET366 |
| B | SER367 |
| B | GLU370 |
| B | HOH610 |
| B | HOH618 |
| B | HOH664 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| A | ASN232 |
| A | HOH604 |
| A | HOH637 |
| B | LYS241 |
| B | GLU274 |
| B | GLY275 |
| B | ILE276 |
| B | HOH639 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | PRO126 |
| B | LYS289 |
| B | VAL291 |
| B | LEU478 |
| B | TRP481 |
| B | LYS482 |
| B | CYS483 |
| B | HOH622 |
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 |
