Current Protein Identity:P0AE06
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 2F1M Conformational flexibility in the multidrug efflux system protein AcrA Deposited 2005-11-14 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
45–312(268 aa)
Fragment:residues 45-312
Chain B
45–312(268 aa)
Fragment:residues 45-312
|
Mutation:F223M, L224M, L287M, L288M Non-standard monomer:Yes (specific site not provided by mmCIF) Mutation:F223M, L224M, L287M, L288M Non-standard monomer:Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 5.4;277 K;30% 2-methyl-2,4-pentadiol (MPD), 20 mM MgCl2, 100 mM citrate pH 5.4, 1 mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 5.40
|
Resolution 2.71 Å R-free 0.275 |
| 2F1M Conformational flexibility in the multidrug efflux system protein AcrA Deposited 2005-11-14 | Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain C
45–312(268 aa)
Fragment:residues 45-312
Chain D
45–312(268 aa)
Fragment:residues 45-312
|
Mutation:F223M, L224M, L287M, L288M Non-standard monomer:Yes (specific site not provided by mmCIF) Mutation:F223M, L224M, L287M, L288M Non-standard monomer:Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 5.4;277 K;30% 2-methyl-2,4-pentadiol (MPD), 20 mM MgCl2, 100 mM citrate pH 5.4, 1 mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 5.40
|
Resolution 2.71 Å R-free 0.275 |
| 5NG5 multi-drug efflux; membrane transport; RND superfamily; Drug resistance Deposited 2017-03-16 | Assembly 1 Protein heterocomplex Heteromer;Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein count |
Chain A
25–397(373 aa)
Chain B
25–397(373 aa)
Chain D
25–397(373 aa)
Chain E
25–397(373 aa)
Chain G
25–397(373 aa)
Chain H
25–397(373 aa)
|
Not recorded | 5QF 6-[2-(3,4-dimethoxyphenyl)ethylsulfanyl]-8-[4-(2-methoxyethyl)piperazin-1-yl]-3,3-dimethyl-1,4-dihydropyrano[3,4-c]pyridine-5-carbonitrile × 3 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE;a 3ul aliquot at a concentration of 2 mg per ml was applied onto glow-discharged holey carbon grid (Quantifoil Au R1.21.3, 300 mesh)
|
Resolution 6.50 Å |
| 9TG4 Structure of the YbjP lipoprotein bound to the AcrABZ-TolC efflux pump Deposited 2025-11-28 | Assembly 1 Protein heterocomplex Heteromer;Protein × 18 PDB declaration: 18-meric(18) Consistent with protein count |
Chain D
1–397(397 aa)
Chain E
1–397(397 aa)
Chain F
1–397(397 aa)
Chain G
1–397(397 aa)
Chain H
1–397(397 aa)
Chain I
1–397(397 aa)
|
Not recorded | CL CHLORIDE ION × 3 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.17 Å |
| 9V53 Structure of TolC, YbjP, and AcrABZ complex Deposited 2025-05-25 | Assembly 1 Protein heterocomplex Heteromer;Protein × 18 PDB declaration: octadecameric(18) Consistent with protein count |
Chain A1
1–397(397 aa)
Chain A2
1–397(397 aa)
Chain A3
1–397(397 aa)
Chain a1
1–397(397 aa)
Chain a2
1–397(397 aa)
Chain a3
1–397(397 aa)
|
Not recorded | No recorded non-water small molecule | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen NITROGEN
|
Resolution 3.39 Å |
| 9V55 Structure of TolC, YbjP, and AcrA complex Deposited 2025-05-25 | Assembly 1 Protein heterocomplex Heteromer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count |
Chain A1
1–397(397 aa)
Chain A2
1–397(397 aa)
Chain A3
1–397(397 aa)
Chain a1
1–397(397 aa)
Chain a2
1–397(397 aa)
Chain a3
1–397(397 aa)
|
Not recorded | No recorded non-water small molecule | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen NITROGEN
|
Resolution 3.26 Å |