Structure analysis

Cryo-EM structure of an Acinetobacter baumannii multidrug efflux pump

Electron Microscopy
2.98Å resolution
Source organism: Acinetobacter baumannii
Assembly composition:
homo trimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo trimer
Accessible surface area: 121940.46 Å2
Buried surface area: 22356.23 Å2
Dissociation area: 8,926.84 Å2
Dissociation energy (ΔGdiss): 100.66 kcal/mol
Dissociation entropy (TΔSdiss): 35.2 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-173394

Macromolecules

Chains: A, B, C
Length: 1035 amino acids
Theoretical weight: 112.59 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2FD70 (Residues: 2-1036; Coverage: 100%)
Gene names: 32_436, DWA16_01010, EA686_00900, GNY86_15955, adeB
Pfam: AcrB/AcrD/AcrF family
InterPro:
PDBe-KB: UniProt Coverage View: Q2FD70  
110351002003004005006007008009001,000
 
5001000MSQFFIRRPVFAWVIAIFIIIFGLLSIPKLPIARFPSVAPPQVNISATYPGATAKTINDSVVTLIERELSGVKNLLYYSATTDTSGTAEITATFKPGTDVEMAQVDVQNKIKAVEARLPQVVRQQGLQVEASSSGFLMLVGINSPNNQYSEVDLSDYLVRNVVEELKRVEGVGKVQSFGAEKAMRIWVDPNKLVSYGLSISDVNNAIRENNVEIAPGRLGDLPAEKGQLITIPLSAQGQLSSLEQFKNISLKSKTNGSVIKLSDVANVEIGSQAYNFAILENGKPATAAAIQLSPGANAVKTAEGVRAKIEELKLNLPEGMEFSIPYDTAPFVKISIEKVIHTLLEAMVLVFIVMYLFLHNVRYTLIPAIVAPIALLGTFTVMLLAGFSINVLTMFGMVLAIGIIVDDAIVVVENVERIMATEGLSPKDATSKAMKEITSPIIGITLVLAAVFLPMAFASGSVGVIYKQFTLTMSVSILFSALLALILTPALCATILKPIDGHHQKKGFFAWFDRSFDKVTKKYELMLLKIIKHTVPMMVIFLVITGITFAGMKYWPTAFMPEEDQGWFMTSFQLPSDATAERTRNVVNQFENNLKDNPDVKSNTAILGWGFSGAGQNVAVAFTTLKDFKERTSSASKMTSDVNSSMANSTEGETMAVLPPAIDELGTFSGFSLRLQDRANLGMPALLAAQDELMAMAAKNKKFYMVWNEGLPQGDNISLKIDREKLSALGVKFSDVSDIISTSMGSMYINDFPNQGRMQQVIVQVEAKSRMQLKDILNLKVMGSSGQLVSLSEVVTPQWNKAPQQYNRYNGRPSLSIAGIPNFDTSSGEAMREMEQLIAKLPKGIGYEWTGISLQEKQSESQMAFLLGLSMLVVFLVLAALYESWAIPLSVMLVVPLGIFGAIIAIMSRGLMNDVFFKIGLITIIGLSAKNAILIVEFAKMLKEEGMSLIEATVAAAKLRLRPILMTSLAFTCGVIPLVIATGASSETQHALGTGVFGGMISATILAIFFVPVFFIFILGAVEKLFSSKKKISS
UniProt
Q2FD70
Chains
Domains
Secondary structure
Flexibility predictions
Ligand binding sites
Interaction interfaces
Sequence conservation

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