5N6L
Structure of the membrane integral lipoprotein N-acyltransferase Lnt C387A mutant from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0016410 | molecular_function | N-acyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042158 | biological_process | lipoprotein biosynthetic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0016020 | cellular_component | membrane |
| B | 0016410 | molecular_function | N-acyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042158 | biological_process | lipoprotein biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 601 |
| Chain | Residue |
| A | ALA22 |
| A | THR25 |
| A | LEU26 |
| A | TYR31 |
| A | SER70 |
| A | ASN73 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue OLC A 602 |
| Chain | Residue |
| A | ALA46 |
| A | LEU47 |
| A | PHE49 |
| A | ASN50 |
| A | GLU8 |
| A | ARG13 |
| A | PHE20 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 603 |
| Chain | Residue |
| A | TRP121 |
| A | MET178 |
| A | LEU182 |
| A | ASN191 |
| A | VAL197 |
| A | OLC617 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 604 |
| Chain | Residue |
| A | ARG190 |
| A | ASN191 |
| A | LEU195 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 605 |
| Chain | Residue |
| A | GLN10 |
| A | LEU14 |
| A | ARG52 |
| A | GLN55 |
| A | PHE61 |
| A | OLC619 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 606 |
| Chain | Residue |
| A | ASN488 |
| A | TRP489 |
| A | TRP492 |
| A | OLC608 |
| A | OLC617 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 607 |
| Chain | Residue |
| A | ARG11 |
| A | LEU18 |
| A | PHE65 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 608 |
| Chain | Residue |
| A | PHE137 |
| A | GLU170 |
| A | ASN488 |
| A | TRP492 |
| A | OLC606 |
| A | OLC614 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 609 |
| Chain | Residue |
| A | LEU208 |
| A | TRP213 |
| A | ARG485 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 610 |
| Chain | Residue |
| A | PHE341 |
| A | PRO361 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 611 |
| Chain | Residue |
| A | LEU18 |
| A | ASN73 |
| A | TYR76 |
| A | VAL94 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue OLC A 612 |
| Chain | Residue |
| A | ILE79 |
| A | LEU97 |
| A | VAL339 |
| A | PHE341 |
| A | PHE416 |
| A | OLC613 |
| A | OLC618 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 613 |
| Chain | Residue |
| A | PHE82 |
| A | PHE341 |
| A | TRP415 |
| A | OLC612 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 614 |
| Chain | Residue |
| A | TRP141 |
| A | OLC608 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 615 |
| Chain | Residue |
| A | LEU26 |
| A | PRO30 |
| A | TYR31 |
| A | PRO356 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 616 |
| Chain | Residue |
| A | VAL196 |
| A | VAL200 |
| A | ALA203 |
| A | LEU497 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 617 |
| Chain | Residue |
| A | VAL197 |
| A | LEU201 |
| A | LEU204 |
| A | OLC603 |
| A | OLC606 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 618 |
| Chain | Residue |
| A | PHE146 |
| A | VAL339 |
| A | PRO340 |
| A | OLC612 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 619 |
| Chain | Residue |
| A | LEU54 |
| A | OLC605 |
| B | ILE211 |
| B | GLN212 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 620 |
| Chain | Residue |
| A | GLY258 |
| A | LYS259 |
| A | SER261 |
| A | GLY292 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 621 |
| Chain | Residue |
| A | TRP141 |
| A | LEU143 |
| A | GOL622 |
| site_id | AE4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 622 |
| Chain | Residue |
| A | THR144 |
| A | PRO346 |
| A | LEU347 |
| A | GOL621 |
| site_id | AE5 |
| Number of Residues | 1 |
| Details | binding site for residue GOL A 623 |
| Chain | Residue |
| A | PHE92 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 624 |
| Chain | Residue |
| A | ARG9 |
| A | GLN10 |
| site_id | AE7 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 625 |
| Chain | Residue |
| A | GOL626 |
| A | HOH705 |
| site_id | AE8 |
| Number of Residues | 1 |
| Details | binding site for residue GOL A 626 |
| Chain | Residue |
| A | GOL625 |
| site_id | AE9 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 627 |
| Chain | Residue |
| A | PHE202 |
| A | PHE206 |
| site_id | AF1 |
| Number of Residues | 5 |
| Details | binding site for residue OLC B 601 |
| Chain | Residue |
| B | ALA22 |
| B | LEU26 |
| B | TYR31 |
| B | SER70 |
| B | ASN73 |
| site_id | AF2 |
| Number of Residues | 6 |
| Details | binding site for residue OLC B 602 |
| Chain | Residue |
| A | PRO86 |
| A | VAL89 |
| A | PHE92 |
| B | MET178 |
| B | LEU494 |
| B | PHE498 |
| site_id | AF3 |
| Number of Residues | 5 |
| Details | binding site for residue OLC B 603 |
| Chain | Residue |
| B | ILE7 |
| B | ARG13 |
| B | ALA46 |
| B | LEU47 |
| B | PHE49 |
| site_id | AF4 |
| Number of Residues | 6 |
| Details | binding site for residue OLC B 604 |
| Chain | Residue |
| B | VAL134 |
| B | GLU394 |
| B | ASN488 |
| B | TRP489 |
| B | TRP492 |
| B | GLY499 |
| site_id | AF5 |
| Number of Residues | 3 |
| Details | binding site for residue OLC B 605 |
| Chain | Residue |
| B | LEU54 |
| B | LEU96 |
| B | LEU103 |
| site_id | AF6 |
| Number of Residues | 3 |
| Details | binding site for residue OLC B 606 |
| Chain | Residue |
| B | TYR210 |
| B | ILE211 |
| B | GLN212 |
| site_id | AF7 |
| Number of Residues | 1 |
| Details | binding site for residue OLC B 607 |
| Chain | Residue |
| B | ARG209 |
| site_id | AF8 |
| Number of Residues | 4 |
| Details | binding site for residue OLC B 608 |
| Chain | Residue |
| B | PHE137 |
| B | TRP141 |
| B | ASN488 |
| B | TRP492 |
| site_id | AF9 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 609 |
| Chain | Residue |
| B | TRP141 |
| B | LEU143 |
| B | THR144 |
| site_id | AG1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 610 |
| Chain | Residue |
| A | GLU239 |
| A | GLN277 |
| B | GLN277 |
| B | PHE280 |
| site_id | AG2 |
| Number of Residues | 1 |
| Details | binding site for residue GOL B 611 |
| Chain | Residue |
| B | ASP32 |
| site_id | AG3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 612 |
| Chain | Residue |
| A | LYS247 |
| A | ASN251 |
| B | ASN244 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 306 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 372 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28885614","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28885614","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 249 |
| Details | Domain: {"description":"CN hydrolase","evidences":[{"source":"HAMAP-Rule","id":"MF_01148","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01148","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01148","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01148","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
