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4KX6

Plasticity of the quinone-binding site of the complex II homolog quinol:fumarate reductase

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, E
(A, M)
Fumarate reductase flavoprotein subunitpolymer57763477.72UniProt (P00363)
Pfam (PF00890)
Pfam (PF02910)
Escherichia coli
2B, F
(B, N)
Fumarate reductase (Anaerobic), Fe-S subunitpolymer24327021.92UniProt (C5A1E7)Escherichia coli
3C, G
(C, O)
Fumarate reductase subunit Cpolymer13014882.82UniProt (C9QU46)Escherichia coliFumarate reductase 15 kDa hydrophobic protein
4D, H
(D, P)
Fumarate reductase subunit Dpolymer11913118.92UniProt (P0A8Q3)
Pfam (PF02313)
Escherichia coliFumarate reductase 13 kDa hydrophobic protein
5I, N
(A, M)
FLAVIN-ADENINE DINUCLEOTIDEnon-polymer785.52Chemie (FAD)
6J, O
(B, N)
FE2/S2 (INORGANIC) CLUSTERnon-polymer175.82Chemie (FES)
7K, P
(B, N)
FE3-S4 CLUSTERnon-polymer295.82Chemie (F3S)
8L, Q
(B, N)
IRON/SULFUR CLUSTERnon-polymer351.62Chemie (SF4)
9M, R
(D, N)
MENAQUINONE-7non-polymer649.02Chemie (MQ7)
Sequence modifications
C, O: 1 - 130 (UniProt: C9QU46)
PDBExternal DatabaseDetails
Leu 29Glu 30engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains8
Total formula weight237002.6
Non-Polymers*Number of molecules10
Total formula weight4515.6
All*Total formula weight241518.2
*Water molecules are not included.

247947

PDB entries from 2026-01-21

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