4MQY
Crystal Structure of the Escherichia coli LpxC/LPC-138 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019213 | molecular_function | deacetylase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0103117 | molecular_function | UDP-3-O-acyl-N-acetylglucosamine deacetylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS79 |
| A | HIS238 |
| A | ASP242 |
| A | 2CW402 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 2CW A 402 |
| Chain | Residue |
| A | THR191 |
| A | PHE192 |
| A | ILE198 |
| A | GLN202 |
| A | GLY210 |
| A | SER211 |
| A | PHE212 |
| A | ALA215 |
| A | HIS238 |
| A | ASP242 |
| A | HIS265 |
| A | ZN401 |
| A | SO4404 |
| A | HOH511 |
| A | HOH666 |
| A | LEU18 |
| A | LEU62 |
| A | CYS63 |
| A | GLU78 |
| A | HIS79 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE DMS A 403 |
| Chain | Residue |
| A | HOH649 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 404 |
| Chain | Residue |
| A | ASP59 |
| A | LYS239 |
| A | GLY264 |
| A | HIS265 |
| A | 2CW402 |
| A | HOH511 |
| A | HOH553 |
| A | HOH638 |
| A | HOH666 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 405 |
| Chain | Residue |
| A | GLU122 |
| A | LEU123 |
| A | ASN124 |
| A | HOH587 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 406 |
| Chain | Residue |
| A | LYS22 |
| A | LYS23 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 407 |
| Chain | Residue |
| A | LYS8 |
| A | ARG9 |
| A | ARG204 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 408 |
| Chain | Residue |
| A | CYS250 |
| A | TYR284 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE UKW A 409 |
| Chain | Residue |
| A | MET61 |
| A | TYR113 |
| A | MET183 |
| A | SER187 |
| A | ARG188 |
| A | PHE194 |
| A | ASP197 |
| A | LEU201 |
| A | ALA302 |
| A | HOH575 |
| A | HOH606 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15705580","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24108127","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24108127","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24117400","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
