3D9B
Symmetric structure of E. coli AcrB
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0009636 | biological_process | response to toxic substance |
A | 0015125 | molecular_function | bile acid transmembrane transporter activity |
A | 0015562 | molecular_function | efflux transmembrane transporter activity |
A | 0015567 | molecular_function | alkane transmembrane transporter activity |
A | 0015721 | biological_process | bile acid and bile salt transport |
A | 0015895 | biological_process | alkane transport |
A | 0015908 | biological_process | fatty acid transport |
A | 0016020 | cellular_component | membrane |
A | 0022857 | molecular_function | transmembrane transporter activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0042908 | biological_process | xenobiotic transport |
A | 0042910 | molecular_function | xenobiotic transmembrane transporter activity |
A | 0042930 | biological_process | enterobactin transport |
A | 0042931 | molecular_function | enterobactin transmembrane transporter activity |
A | 0046677 | biological_process | response to antibiotic |
A | 0055085 | biological_process | transmembrane transport |
A | 0098567 | cellular_component | periplasmic side of plasma membrane |
A | 0140330 | biological_process | xenobiotic detoxification by transmembrane export across the cell outer membrane |
A | 1990281 | cellular_component | efflux pump complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NI A 1201 |
Chain | Residue |
A | HIS525 |
A | ASP529 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 124 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | Transmembrane: {"description":"Helical; Name=1"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 644 |
Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 19 |
Details | Transmembrane: {"description":"Helical; Name=2"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 19 |
Details | Transmembrane: {"description":"Helical; Name=3"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=4"} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 18 |
Details | Transmembrane: {"description":"Helical; Name=5"} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 24 |
Details | Transmembrane: {"description":"Helical; Name=6"} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 16 |
Details | Transmembrane: {"description":"Helical; Name=7"} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 16 |
Details | Transmembrane: {"description":"Helical; Name=8"} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 19 |
Details | Transmembrane: {"description":"Helical; Name=9"} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 18 |
Details | Transmembrane: {"description":"Helical; Name=10"} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 19 |
Details | Transmembrane: {"description":"Helical; Name=11"} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 19 |
Details | Transmembrane: {"description":"Helical; Name=12"} |
Chain | Residue | Details |