5O9T
HsNMT1 in complex with CoA and acetylated-NCFSKPK peptide
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | binding site for residue MYA A 501 |
| Chain | Residue |
| A | ARG115 |
| A | ASN246 |
| A | PHE247 |
| A | LEU248 |
| A | CYS249 |
| A | VAL250 |
| A | ARG255 |
| A | SER256 |
| A | ARG258 |
| A | VAL259 |
| A | ALA260 |
| A | TYR117 |
| A | PRO261 |
| A | THR268 |
| A | TYR281 |
| A | THR282 |
| A | LEU287 |
| A | TYR479 |
| A | HOH673 |
| C | 1IP1 |
| A | GLN118 |
| A | PHE119 |
| A | TRP120 |
| A | ASN179 |
| A | TYR180 |
| A | VAL181 |
| A | ILE245 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | GLU244 |
| A | TRP374 |
| A | TYR423 |
| A | LEU493 |
| A | VAL494 |
| A | LEU495 |
| A | GLN496 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | LYS289 |
| A | PRO290 |
| A | VAL291 |
| A | LEU478 |
| A | TRP481 |
| A | LYS482 |
| A | CYS483 |
| A | SER485 |
| A | HOH649 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| A | LEU161 |
| A | LEU163 |
| A | ARG202 |
| A | TRP206 |
| A | HIS211 |
| site_id | AC5 |
| Number of Residues | 32 |
| 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 | ARG258 |
| B | VAL259 |
| B | ALA260 |
| B | PRO261 |
| B | THR268 |
| B | PHE277 |
| B | TYR281 |
| B | THR282 |
| B | LEU287 |
| B | TYR479 |
| B | HOH616 |
| B | HOH653 |
| B | HOH700 |
| B | HOH712 |
| B | HOH717 |
| B | HOH733 |
| D | 1IP1 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | PRO126 |
| B | LYS289 |
| B | VAL291 |
| B | LEU478 |
| B | TRP481 |
| B | LYS482 |
| B | CYS483 |
| B | HOH664 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | GLU244 |
| B | PRO364 |
| B | MET366 |
| B | TRP374 |
| B | TYR423 |
| B | VAL494 |
| B | GLN496 |
| B | HOH683 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 504 |
| Chain | Residue |
| B | HIS211 |
| B | LEU163 |
| B | ARG202 |
| B | TRP206 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide 1IP C 1 and CYS C 2 |
| Chain | Residue |
| A | TYR180 |
| A | PHE190 |
| A | TYR192 |
| A | ASN246 |
| A | THR282 |
| A | ALA283 |
| A | GLY284 |
| A | TYR296 |
| A | TYR401 |
| A | ASN473 |
| A | GLN496 |
| A | MYA501 |
| A | HOH697 |
| A | HOH701 |
| C | PHE3 |
| C | SER4 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide 1IP D 1 and CYS D 2 |
| Chain | Residue |
| B | PHE190 |
| B | ASN246 |
| B | THR282 |
| B | ALA283 |
| B | TYR296 |
| B | TYR401 |
| B | ASN473 |
| B | LEU474 |
| B | GLN496 |
| B | MYA501 |
| B | HOH640 |
| B | HOH680 |
| B | HOH694 |
| D | PHE3 |
| D | SER4 |
| D | HOH102 |
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 |
