4C2Z
Human N-myristoyltransferase (NMT1) with Myristoyl-CoA and inhibitor bound
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE MYA B 1497 |
| Chain | Residue |
| B | ARG115 |
| B | PHE247 |
| B | LEU248 |
| B | CYS249 |
| B | VAL250 |
| B | ARG255 |
| B | SER256 |
| B | ARG258 |
| B | VAL259 |
| B | ALA260 |
| B | PRO261 |
| B | TYR117 |
| B | THR268 |
| B | TYR281 |
| B | THR282 |
| B | LEU287 |
| B | TYR479 |
| B | 6461498 |
| B | MG1499 |
| B | HOH2127 |
| B | HOH2128 |
| B | HOH2246 |
| B | GLN118 |
| B | HOH2247 |
| B | HOH2248 |
| B | HOH2249 |
| B | HOH2250 |
| B | HOH2251 |
| B | PHE119 |
| B | TRP120 |
| B | TYR180 |
| B | VAL181 |
| B | ILE245 |
| B | ASN246 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE MYA A 1497 |
| Chain | Residue |
| A | TYR117 |
| A | GLN118 |
| A | PHE119 |
| A | TRP120 |
| A | TYR180 |
| A | VAL181 |
| A | ILE245 |
| A | ASN246 |
| A | PHE247 |
| A | LEU248 |
| A | CYS249 |
| A | VAL250 |
| A | ARG255 |
| A | SER256 |
| A | LYS257 |
| A | ARG258 |
| A | VAL259 |
| A | ALA260 |
| A | PRO261 |
| A | THR268 |
| A | VAL271 |
| A | PHE277 |
| A | TYR281 |
| A | THR282 |
| A | LEU287 |
| A | TYR479 |
| A | MG1499 |
| A | HOH2003 |
| A | HOH2163 |
| A | HOH2272 |
| A | HOH2273 |
| A | HOH2274 |
| A | HOH2275 |
| A | HOH2276 |
| A | HOH2278 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 646 A 1498 |
| Chain | Residue |
| A | TYR180 |
| A | VAL181 |
| A | ASP183 |
| A | PHE188 |
| A | PHE190 |
| A | ASN246 |
| A | THR282 |
| A | GLY284 |
| A | TYR296 |
| A | HIS298 |
| A | PHE311 |
| A | SER405 |
| A | TYR420 |
| A | ASP471 |
| A | GLN496 |
| A | HOH2087 |
| A | HOH2176 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 646 B 1498 |
| Chain | Residue |
| B | ASP471 |
| B | GLN496 |
| B | MYA1497 |
| B | HOH2139 |
| B | HOH2140 |
| B | GLU182 |
| B | ASP183 |
| B | ASP184 |
| B | PHE188 |
| B | PHE190 |
| B | ASN246 |
| B | THR282 |
| B | GLY284 |
| B | TYR296 |
| B | HIS298 |
| B | PHE311 |
| B | SER405 |
| B | TYR420 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 1499 |
| Chain | Residue |
| A | LEU254 |
| A | ARG255 |
| A | SER256 |
| A | LYS257 |
| A | ARG258 |
| A | VAL259 |
| A | MYA1497 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1499 |
| Chain | Residue |
| B | LEU254 |
| B | SER256 |
| B | LYS257 |
| B | ARG258 |
| B | VAL259 |
| B | MYA1497 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CIT A 1500 |
| Chain | Residue |
| A | THR122 |
| A | GLN123 |
| A | PRO124 |
| A | GLU139 |
| A | LYS142 |
| A | ARG265 |
| A | ASN389 |
| A | ALA390 |
| A | HOH2018 |
| A | HOH2279 |
| A | HOH2280 |
| A | HOH2281 |
| A | HOH2283 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CIT B 1500 |
| Chain | Residue |
| B | THR122 |
| B | GLN123 |
| B | GLU139 |
| B | LYS142 |
| B | ARG265 |
| B | ASN389 |
| B | ALA390 |
| B | HOH2131 |
| B | HOH2161 |
| B | HOH2206 |
| B | HOH2252 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1501 |
| Chain | Residue |
| A | LYS289 |
| A | VAL291 |
| A | LEU478 |
| A | TRP481 |
| A | LYS482 |
| A | CYS483 |
| A | SER485 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1501 |
| Chain | Residue |
| B | GLU244 |
| B | PRO364 |
| B | MET366 |
| B | TRP374 |
| B | TYR423 |
| B | VAL494 |
| B | GLN496 |
| B | HOH2254 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1502 |
| Chain | Residue |
| A | GLU244 |
| A | MET366 |
| A | TRP374 |
| A | PHE422 |
| A | TYR423 |
| A | VAL494 |
| A | GLN496 |
| A | HOH2156 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 1502 |
| Chain | Residue |
| B | PRO126 |
| B | LYS289 |
| B | VAL291 |
| B | TYR477 |
| B | LEU478 |
| B | TRP481 |
| B | LYS482 |
| B | CYS483 |
| B | HOH2137 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 1503 |
| Chain | Residue |
| B | SER300 |
| B | PRO303 |
| B | SER312 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1503 |
| Chain | Residue |
| A | SER300 |
| A | PRO303 |
| A | SER312 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 1504 |
| Chain | Residue |
| A | GLN118 |
| A | ARG258 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 1504 |
| Chain | Residue |
| B | GLN118 |
| B | ARG258 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 1505 |
| Chain | Residue |
| A | VAL132 |
| A | SER485 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 1505 |
| Chain | Residue |
| B | VAL132 |
| B | LYS289 |
| B | SER485 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 1506 |
| Chain | Residue |
| B | ASP237 |
| B | THR238 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 1507 |
| Chain | Residue |
| B | ARG215 |
| B | ARG220 |
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 |
