5O6H
Human NMT1 in complex with myristoyl-CoA and inhibitor IMP-917
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | binding site for residue MYA A 2001 |
| Chain | Residue |
| A | TYR117 |
| A | LEU248 |
| A | CYS249 |
| A | VAL250 |
| A | ARG255 |
| A | SER256 |
| A | LYS257 |
| A | ARG258 |
| A | VAL259 |
| A | ALA260 |
| A | PRO261 |
| A | GLN118 |
| A | THR268 |
| A | VAL271 |
| A | PHE277 |
| A | TYR281 |
| A | THR282 |
| A | LEU287 |
| A | TYR479 |
| A | MG2006 |
| A | HOH2130 |
| A | HOH2199 |
| A | PHE119 |
| A | HOH2203 |
| A | HOH2274 |
| A | HOH2320 |
| A | HOH2388 |
| A | HOH2391 |
| A | TRP120 |
| A | ASN179 |
| A | TYR180 |
| A | VAL181 |
| A | ASN246 |
| A | PHE247 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 A 2002 |
| Chain | Residue |
| A | GLU139 |
| A | LYS142 |
| A | HOH2156 |
| A | HOH2174 |
| A | HOH2188 |
| A | HOH2237 |
| A | HOH2242 |
| A | HOH2350 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 A 2003 |
| Chain | Residue |
| A | TYR150 |
| A | THR151 |
| A | VAL262 |
| A | ARG265 |
| A | ALA336 |
| A | GLY337 |
| A | LEU338 |
| A | DMS2008 |
| A | HOH2116 |
| A | HOH2152 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue PO4 A 2004 |
| Chain | Residue |
| A | GLN118 |
| A | PHE119 |
| A | ARG258 |
| A | PRO261 |
| A | ARG265 |
| A | LYS334 |
| A | HOH2119 |
| A | HOH2163 |
| A | HOH2434 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue 9M2 A 2005 |
| Chain | Residue |
| A | VAL181 |
| A | PHE188 |
| A | PHE190 |
| A | TYR192 |
| A | ASN246 |
| A | THR282 |
| A | TYR296 |
| A | SER405 |
| A | TYR420 |
| A | ASN451 |
| A | ALA452 |
| A | LEU495 |
| A | GLN496 |
| A | HOH2138 |
| A | HOH2317 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 2006 |
| Chain | Residue |
| A | LEU254 |
| A | SER256 |
| A | LYS257 |
| A | ARG258 |
| A | VAL259 |
| A | MYA2001 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 2007 |
| Chain | Residue |
| A | PRO126 |
| A | LYS289 |
| A | VAL291 |
| A | TYR477 |
| A | LEU478 |
| A | TRP481 |
| A | LYS482 |
| A | CYS483 |
| A | SER485 |
| A | HOH2145 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 2008 |
| Chain | Residue |
| A | LEU338 |
| A | PO42003 |
| A | HOH2187 |
| A | HOH2342 |
| site_id | AC9 |
| Number of Residues | 35 |
| Details | binding site for residue MYA B 2001 |
| Chain | Residue |
| 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 | VAL271 |
| B | PHE277 |
| B | THR282 |
| B | LEU287 |
| B | TYR479 |
| B | MG2008 |
| B | HOH2145 |
| B | HOH2160 |
| B | HOH2212 |
| B | HOH2287 |
| B | HOH2311 |
| B | HOH2371 |
| B | HOH2411 |
| B | HOH2471 |
| B | ARG115 |
| B | TYR117 |
| B | GLN118 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue PO4 B 2002 |
| Chain | Residue |
| B | GLU139 |
| B | LYS142 |
| B | HOH2108 |
| B | HOH2190 |
| B | HOH2205 |
| B | HOH2275 |
| B | HOH2284 |
| B | HOH2307 |
| B | HOH2315 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue PO4 B 2003 |
| Chain | Residue |
| B | TYR150 |
| B | THR151 |
| B | VAL262 |
| B | ARG265 |
| B | ALA336 |
| B | GLY337 |
| B | LEU338 |
| B | GOL2010 |
| B | HOH2115 |
| B | HOH2126 |
| B | HOH2324 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 B 2004 |
| Chain | Residue |
| B | GLN118 |
| B | PHE119 |
| B | ARG258 |
| B | PRO261 |
| B | ARG265 |
| B | LYS334 |
| B | HOH2104 |
| B | HOH2399 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 2005 |
| Chain | Residue |
| B | ARG166 |
| B | LYS170 |
| B | ARG355 |
| B | HOH2144 |
| B | HOH2421 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 2006 |
| Chain | Residue |
| B | GLU372 |
| B | HIS373 |
| B | HOH2129 |
| B | HOH2292 |
| B | HOH2422 |
| site_id | AD6 |
| Number of Residues | 16 |
| Details | binding site for residue 9M2 B 2007 |
| Chain | Residue |
| B | VAL181 |
| B | PHE188 |
| B | PHE190 |
| B | TYR192 |
| B | ASN246 |
| B | THR282 |
| B | TYR296 |
| B | SER405 |
| B | TYR420 |
| B | ASN451 |
| B | ALA452 |
| B | LEU453 |
| B | LEU495 |
| B | GLN496 |
| B | HOH2131 |
| B | HOH2258 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 2008 |
| Chain | Residue |
| B | LEU254 |
| B | SER256 |
| B | LYS257 |
| B | ARG258 |
| B | VAL259 |
| B | MYA2001 |
| site_id | AD8 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 2009 |
| Chain | Residue |
| B | PRO126 |
| B | LYS289 |
| B | PRO290 |
| B | VAL291 |
| B | TYR477 |
| B | LEU478 |
| B | TRP481 |
| B | LYS482 |
| B | CYS483 |
| B | SER485 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 2010 |
| Chain | Residue |
| B | LEU338 |
| B | PRO340 |
| B | PHE385 |
| B | PO42003 |
| B | HOH2465 |
| B | HOH2477 |
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 |
