7KGG
Cryo-EM Structures of AdeB from Acinetobacter baumannii: AdeB-ET-I
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
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 | 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 | 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 | PHE458 |
A | PHE866 |
B | PHE22 |
B | LEU25 |
B | SER26 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue PTY A 1102 |
Chain | Residue |
A | PHE480 |
A | LEU483 |
A | PHE22 |
A | LEU385 |
A | ALA386 |
A | LYS468 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue PTY B 1101 |
Chain | Residue |
B | ALA386 |
B | GLY387 |
B | PHE388 |
B | ALA457 |
B | LYS468 |
B | LEU472 |
B | PHE480 |
B | PTY1102 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue PTY B 1102 |
Chain | Residue |
B | LEU454 |
B | PHE458 |
B | PHE866 |
B | LEU870 |
B | PTY1101 |
C | SER26 |
C | LYS29 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue PTY C 1101 |
Chain | Residue |
A | PHE22 |
A | SER26 |
A | LYS29 |
C | ALA450 |
C | PHE458 |
C | GLN863 |
C | PHE866 |
C | LEU870 |
C | VAL874 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue PTY C 1102 |
Chain | Residue |
C | PHE388 |
C | LYS468 |
C | SER475 |
C | PHE480 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue ET C 1103 |
Chain | Residue |
C | MET656 |
C | TRP708 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue ET C 1104 |
Chain | Residue |
C | PHE178 |
C | PHE277 |
C | TRP610 |
C | ET1105 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue ET C 1105 |
Chain | Residue |
C | LEU139 |
C | TYR327 |
C | TRP568 |
C | ILE607 |
C | PHE623 |
C | THR625 |
C | ET1104 |