6VKS
Cryo-electron microscopy structures of a gonococcal multidrug efflux pump illuminate a mechanism of drug recognition with ampicillin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0009636 | biological_process | response to toxic substance |
A | 0015562 | molecular_function | efflux transmembrane transporter activity |
A | 0016020 | cellular_component | membrane |
A | 0022857 | molecular_function | transmembrane transporter activity |
A | 0042908 | biological_process | xenobiotic transport |
A | 0042910 | molecular_function | xenobiotic transmembrane transporter activity |
A | 0055085 | biological_process | transmembrane transport |
B | 0005886 | cellular_component | plasma membrane |
B | 0009636 | biological_process | response to toxic substance |
B | 0015562 | molecular_function | efflux transmembrane transporter activity |
B | 0016020 | cellular_component | membrane |
B | 0022857 | molecular_function | transmembrane transporter activity |
B | 0042908 | biological_process | xenobiotic transport |
B | 0042910 | molecular_function | xenobiotic transmembrane transporter activity |
B | 0055085 | biological_process | transmembrane transport |
C | 0005886 | cellular_component | plasma membrane |
C | 0009636 | biological_process | response to toxic substance |
C | 0015562 | molecular_function | efflux transmembrane transporter activity |
C | 0016020 | cellular_component | membrane |
C | 0022857 | molecular_function | transmembrane transporter activity |
C | 0042908 | biological_process | xenobiotic transport |
C | 0042910 | molecular_function | xenobiotic transmembrane transporter activity |
C | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue PTY A 1101 |
Chain | Residue |
A | ARG8 |
A | PHE18 |
B | ILE441 |
B | LEU888 |
B | PTY1101 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue PTY A 1102 |
Chain | Residue |
A | TRP13 |
A | ILE17 |
B | PTY1103 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue PTY A 1103 |
Chain | Residue |
A | PHE1040 |
A | THR1043 |
C | PTY1104 |
A | TRP892 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue PTY B 1101 |
Chain | Residue |
A | PTY1101 |
B | MET1 |
B | PHE5 |
B | SER437 |
B | PTY1102 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue PTY B 1102 |
Chain | Residue |
B | PHE11 |
B | PTY1101 |
C | ALA887 |
C | LEU888 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue PTY B 1103 |
Chain | Residue |
A | PTY1102 |
B | PHE882 |
B | TRP892 |
B | LEU896 |
B | LEU899 |
B | PHE1040 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue PTY B 1104 |
Chain | Residue |
B | ALA21 |
B | ALA22 |
B | ILE24 |
B | PHE25 |
C | MET456 |
C | ALA872 |
C | ALA875 |
C | PTY1103 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue PTY B 1105 |
Chain | Residue |
B | ILE27 |
B | ASN296 |
B | ILE335 |
B | LEU374 |
B | PHE378 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue AIX B 1106 |
Chain | Residue |
B | PHE136 |
B | PHE176 |
B | VAL607 |
B | PHE610 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue PTY C 1101 |
Chain | Residue |
A | GLY438 |
A | LEU888 |
A | MET1049 |
C | PHE4 |
C | ARG8 |
C | PHE11 |
C | PHE18 |
C | PTY1102 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue PTY C 1102 |
Chain | Residue |
C | LYS3 |
C | PHE4 |
C | PTY1101 |
C | PTY1107 |
C | PTY1108 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue PTY C 1104 |
Chain | Residue |
A | PTY1103 |
C | ILE17 |
C | PTY1105 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue PTY C 1105 |
Chain | Residue |
C | TRP13 |
C | ARG361 |
C | MET494 |
C | PTY1104 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue PTY C 1106 |
Chain | Residue |
C | ILE27 |
C | ILE343 |
C | PTY1109 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue PTY C 1107 |
Chain | Residue |
C | MET1 |
C | PHE4 |
C | PHE5 |
C | PHE481 |
C | PTY1102 |
C | PTY1108 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue PTY C 1108 |
Chain | Residue |
C | PTY1102 |
C | PTY1107 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue PTY C 1109 |
Chain | Residue |
C | ILE339 |
C | LEU374 |
C | MET393 |
C | PTY1106 |
site_id | AD9 |
Number of Residues | 13 |
Details | binding site for Di-peptide PTY C 1103 and PHE C 1040 |
Chain | Residue |
B | PTY1104 |
C | VAL879 |
C | PHE882 |
C | SER891 |
C | TRP892 |
C | SER893 |
C | LEU896 |
C | VAL1036 |
C | ARG1037 |
C | LYS1038 |
C | PHE1039 |
C | LYS1041 |
C | GLU1042 |