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4G39

Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A
(A)
Sulfite reductase [NADPH] hemoprotein beta-componentpolymer57064021.01UniProt (P17846)
Pfam (PF03460)
Pfam (PF01077)
Escherichia coliSiR-HP, SiRHP
2B
(A)
PHOSPHATE IONnon-polymer95.01Chemie (PO4)
3C, D
(A)
POTASSIUM IONnon-polymer39.12Chemie (K)
4E
(A)
IRON/SULFUR CLUSTERnon-polymer351.61Chemie (SF4)
5F
(A)
SIROHEMEnon-polymer916.71Chemie (SRM)
6G
(A)
waterwater18.0117Chemie (HOH)
Sequence modifications
A: 81 - 570 (UniProt: P17846)
PDBExternal DatabaseDetails
Ser 153Arg 153engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains1
Total formula weight64021.0
Non-Polymers*Number of molecules5
Total formula weight1441.5
All*Total formula weight65462.4
*Water molecules are not included.

247536

PDB entries from 2026-01-14

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