Current Protein Identity:P0AE06 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

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