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7CH0

The overall structure of the MlaFEDB complex in ATP-bound EQclose conformation (Mutation of E170Q on MlaF)

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, DLipid asymmetry maintenance ABC transporter permease subunit MlaEpolymer26027885.22UniProt (A0A4S5B3V0)
Pfam (PF02405)
UniProt (by SIFTS) (P64606)
In PDB
Escherichia coli K-12
2B, EPhospholipid ABC transporter ATP-binding protein MlaFpolymer26929127.82UniProt (A0A4V3YUQ9)
Pfam (PF00005)
UniProt (by SIFTS) (P63386)
In PDB
Escherichia coli K-12
3C, FLipid asymmetry maintenance protein MlaBpolymer9710690.32UniProt (A0A4S5B5E3)
Pfam (PF13466)
UniProt (by SIFTS) (P64602)
In PDB
Escherichia coli K-12
4G, H, I, J, K...Outer membrane lipid asymmetry maintenance protein MlaDpolymer18319593.16UniProt (A0A6D2XU65)
Pfam (PF02470)
UniProt (by SIFTS) (P64604)
In PDB
Escherichia coli K-12
5B, EADENOSINE-5'-TRIPHOSPHATEnon-polymer507.22Chemie (ATP)
Sequence modifications
B, E: 1 - 269 (UniProt: A0A4V3YUQ9)
PDBExternal DatabaseDetails
Gln 170Glu 170engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains12
Total formula weight252965.4
Non-Polymers*Number of molecules2
Total formula weight1014.4
All*Total formula weight253979.7
*Water molecules are not included.

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PDB entries from 2024-05-29

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