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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：Q9RFD6 New Search
4PDB entries
5Biological assembly
16chain/assembly records
UNP PDB Protein and construct Assembly Composition class Protein state Molecular copy count PDB declaration Consistency status
Q9RFD6 3fwy Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain A Reference sequence 2–297 1 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count
Q9RFD6 3fwy Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain B Reference sequence 2–297 1 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count
Q9RFD6 6uyk Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain A Reference sequence 1–297 1 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count
Q9RFD6 6uyk Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain B Reference sequence 1–297 1 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count
Q9RFD6 6uyk Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain C Reference sequence 1–297 1 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count
Q9RFD6 6uyk Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain D Reference sequence 1–297 1 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count
Q9RFD6 6uyk Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain A Reference sequence 1–297 2 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count
Q9RFD6 6uyk Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain B Reference sequence 1–297 2 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count
Q9RFD6 6uyk Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain C Reference sequence 1–297 2 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count
Q9RFD6 6uyk Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain D Reference sequence 1–297 2 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count
Q9RFD6 8vqj Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain E Reference sequence 1–297 1 Protein heterocomplex Heteromer Protein 6 hexameric （6） Consistent with protein count
Q9RFD6 8vqj Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain F Reference sequence 1–297 1 Protein heterocomplex Heteromer Protein 6 hexameric （6） Consistent with protein count
Q9RFD6 9buo Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain E Reference sequence 1–297 1 Protein heterocomplex Heteromer Protein 8 octameric （8） Consistent with protein count
Q9RFD6 9buo Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain F Reference sequence 1–297 1 Protein heterocomplex Heteromer Protein 8 octameric （8） Consistent with protein count
Q9RFD6 9buo Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain G Reference sequence 1–297 1 Protein heterocomplex Heteromer Protein 8 octameric （8） Consistent with protein count
Q9RFD6 9buo Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein Author chain H Reference sequence 1–297 1 Protein heterocomplex Heteromer Protein 8 octameric （8） Consistent with protein count

“Homomeric versus heteromeric classification follows protein identity; different constructs of the same UniProt entry still require comparison of reference-sequence ranges, mutations and missing segments. Assemblies marked for review remain visible but are not included in the highest-confidence candidate set.