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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, MFumarate reductase flavoprotein subunitpolymer57763477.72UniProt (P00363)
Pfam (PF00890)
Pfam (PF02910)
In PDB
Escherichia coli
2B, NFumarate reductase (Anaerobic), Fe-S subunitpolymer24327021.92UniProt (C5A1E7)
In PDB
Escherichia coli
3C, OFumarate reductase subunit Cpolymer13014882.82UniProt (C9QU46)
In PDB
Escherichia coliFumarate reductase 15 kDa hydrophobic protein
4D, PFumarate reductase subunit Dpolymer11913118.92UniProt (P0A8Q3)
Pfam (PF02313)
In PDB
Escherichia coliFumarate reductase 13 kDa hydrophobic protein
5A, MFLAVIN-ADENINE DINUCLEOTIDEnon-polymer785.52Chemie (FAD)
6B, NFE2/S2 (INORGANIC) CLUSTERnon-polymer175.82Chemie (FES)
7B, NFE3-S4 CLUSTERnon-polymer295.82Chemie (F3S)
8B, NIRON/SULFUR CLUSTERnon-polymer351.62Chemie (SF4)
9D, NMENAQUINONE-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.

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PDB entries from 2024-07-24

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