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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, D
(A, D)
Lipid asymmetry maintenance ABC transporter permease subunit MlaEpolymer26027885.22UniProt (A0A4S5B3V0)
Pfam (PF02405)
UniProt (by SIFTS) (P64606)
Escherichia coli K-12
2B, C
(B, E)
Phospholipid ABC transporter ATP-binding protein MlaFpolymer26929127.82UniProt (A0A4V3YUQ9)
Pfam (PF00005)
UniProt (by SIFTS) (P63386)
Escherichia coli K-12
3E, F
(C, F)
Lipid asymmetry maintenance protein MlaBpolymer9710690.32UniProt (A0A4S5B5E3)
Pfam (PF13466)
UniProt (by SIFTS) (P64602)
Escherichia coli K-12
4G, H, I, J, K...
(G, H, I, J, K...)
Outer membrane lipid asymmetry maintenance protein MlaDpolymer18319593.16UniProt (A0A6D2XU65)
Pfam (PF02470)
UniProt (by SIFTS) (P64604)
Escherichia coli K-12
5M, N
(B, E)
ADENOSINE-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 2025-08-27

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