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4G38

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-componentpolymer57064163.21UniProt (P17846)
Pfam (PF03460)
Pfam (PF01077)
Escherichia coliSiR-HP, SiRHP
2B
(A)
PHOSPHATE IONnon-polymer95.01Chemie (PO4)
3C
(A)
POTASSIUM IONnon-polymer39.11Chemie (K)
4D
(A)
IRON/SULFUR CLUSTERnon-polymer351.61Chemie (SF4)
5E
(A)
SIROHEMEnon-polymer916.71Chemie (SRM)
6F
(A)
waterwater18.0564Chemie (HOH)
Sequence modifications
A: 74 - 570 (UniProt: P17846)
PDBExternal DatabaseDetails
Trp 149Asn 149engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains1
Total formula weight64163.2
Non-Polymers*Number of molecules4
Total formula weight1402.4
All*Total formula weight65565.6
*Water molecules are not included.

247536

PDB entries from 2026-01-14

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