5H92

Crystal structure of the complex between maize Sulfite Reductase and ferredoxin in the form-3 crystal

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C	d5h92c_	Alpha and beta proteins (a+b)	beta-Grasp (ubiquitin-like)	2Fe-2S ferredoxin-like	2Fe-2S ferredoxin-related	2Fe-2S ferredoxin	Maize (Zea mays ) [TaxId: 4577 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	2Fe-2S ferredoxin-like	8034525	3000113	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF03460	e5h92A4	A: a+b two layers	X: Alpha-beta plaits	H: Sulfite reductase, domains 1 and 3 (From Topology)	T: Sulfite reductase, domains 1 and 3	F: PF03460	ECOD (1.6)
A	PF01077	e5h92A3	A: a+b three layers	X: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 (From Topology)	H: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 (From Topology)	T: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4	F: PF01077	ECOD (1.6)
B	PF03460	e5h92B3	A: a+b two layers	X: Alpha-beta plaits	H: Sulfite reductase, domains 1 and 3 (From Topology)	T: Sulfite reductase, domains 1 and 3	F: PF03460	ECOD (1.6)
B	PF01077	e5h92B2	A: a+b three layers	X: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 (From Topology)	H: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 (From Topology)	T: Sulfite reductase hemoprotein (SiRHP), domains 2 and 4	F: PF01077	ECOD (1.6)
C	PF00111	e5h92C1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: PF00111	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.413.10	Alpha Beta	2-Layer Sandwich	Sulfite Reductase Hemoprotein	domain 1	CATH (4.3.0)
B	3.30.413.10	Alpha Beta	2-Layer Sandwich	Sulfite Reductase Hemoprotein	domain 1	CATH (4.3.0)
C	3.10.20.30	Alpha Beta	Roll	Ubiquitin-like (UB roll)	Beta-grasp domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03460	Nitrite/Sulfite reductase ferredoxin-like half domain (NIR_SIR_ferr)	Nitrite/Sulfite reductase ferredoxin-like half domain	-	Repeat
A, B	PF01077	Nitrite and sulphite reductase 4Fe-4S domain (NIR_SIR)	Nitrite and sulphite reductase 4Fe-4S domain	-	Family
C	PF00111	2Fe-2S iron-sulfur cluster binding domain (Fer2)	2Fe-2S iron-sulfur cluster binding domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Sulfite reductase [ferredoxin], chloroplastic	DNA binding binding organic cyclic compound binding nucleic acid binding double-stranded DNA binding tetrapyrrole binding heme binding oxidoreductase activity, acting on a sulfur group of donors oxidoreductase activity sulfite reductase activity catalytic activity oxidoreductase activity, acting on a sulfur group of donors, iron-sulfur protein as acceptor sulfite reductase (ferredoxin) activity iron-sulfur cluster binding DNA binding binding organic cyclic compound binding nucleic acid binding double-stranded DNA binding tetrapyrrole binding heme binding oxidoreductase activity, acting on a sulfur group of donors oxidoreductase activity sulfite reductase activity catalytic activity oxidoreductase activity, acting on a sulfur group of donors, iron-sulfur protein as acceptor sulfite reductase (ferredoxin) activity iron-sulfur cluster binding 4 iron, 4 sulfur cluster binding metal cluster binding small molecule binding cation binding ion binding metal ion binding	regulation of cellular process negative regulation of biological process negative regulation of cellular metabolic process regulation of primary metabolic process negative regulation of RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription regulation of RNA metabolic process organic substance biosynthetic process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process negative regulation of DNA-templated transcription regulation of biological process cellular metabolic process regulation of cellular process negative regulation of biological process negative regulation of cellular metabolic process regulation of primary metabolic process negative regulation of RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription regulation of RNA metabolic process organic substance biosynthetic process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process negative regulation of DNA-templated transcription regulation of biological process cellular metabolic process negative regulation of metabolic process primary metabolic process regulation of cellular metabolic process negative regulation of cellular biosynthetic process organic cyclic compound metabolic process regulation of gene expression biosynthetic process negative regulation of macromolecule biosynthetic process organic cyclic compound biosynthetic process metabolic process regulation of macromolecule biosynthetic process macromolecule metabolic process regulation of DNA-templated transcription regulation of metabolic process negative regulation of RNA metabolic process cellular biosynthetic process RNA metabolic process RNA biosynthetic process nucleic acid biosynthetic process organic substance metabolic process negative regulation of cellular process regulation of RNA biosynthetic process negative regulation of macromolecule metabolic process regulation of biosynthetic process biological regulation regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process regulation of cellular biosynthetic process negative regulation of biosynthetic process cellular process response to stimulus response to stress response to abiotic stimulus response to cold response to temperature stimulus cellular component organization plastid chromosome packaging organelle organization chromosome organization cellular component organization or biogenesis sulfate assimilation sulfur compound metabolic process	membrane-bounded organelle intracellular anatomical structure plastid plastid nucleoid nucleoid cellular anatomical entity intracellular membrane-bounded organelle intracellular organelle chloroplast nucleoid plastid stroma organelle intracellular non-membrane-bounded organelle chloroplast stroma cytoplasm membrane-bounded organelle intracellular anatomical structure plastid plastid nucleoid nucleoid cellular anatomical entity intracellular membrane-bounded organelle intracellular organelle chloroplast nucleoid plastid stroma organelle intracellular non-membrane-bounded organelle chloroplast stroma cytoplasm non-membrane-bounded organelle chloroplast protein-containing complex catalytic complex sulfite reductase complex (NADPH) intracellular protein-containing complex stromule organelle envelope plastid envelope
C	Ferredoxin-1, chloroplastic	iron-sulfur cluster binding 2 iron, 2 sulfur cluster binding binding metal cluster binding small molecule binding electron transfer activity cation binding ion binding metal ion binding	cellular metabolic process electron transport chain metabolic process cellular process generation of precursor metabolites and energy response to light stimulus response to stimulus response to radiation response to abiotic stimulus	membrane-bounded organelle intracellular organelle intracellular anatomical structure plastid organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle chloroplast plastid stroma chloroplast stroma

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR005117	Nitrite/Sulfite reductase ferredoxin-like domain	Domain
A, B	IPR011787	Sulphite reductase, ferredoxin dependent	Family
A, B	IPR006067	Nitrite/sulphite reductase 4Fe-4S domain	Domain
A, B	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site	Binding Site
A, B	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily	Homologous Superfamily
A, B	IPR036136	Nitrite/Sulfite reductase ferredoxin-like domain superfamily	Homologous Superfamily
A, B	IPR045169	Nitrite and sulphite reductase 4Fe-4S domain containing protein	Family
C	IPR036010	2Fe-2S ferredoxin-like superfamily	Homologous Superfamily
C	IPR010241	Ferredoxin [2Fe-2S], plant	Family
C	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain	Domain
C	IPR012675	Beta-grasp domain superfamily	Homologous Superfamily
C	IPR006058	2Fe-2S ferredoxin, iron-sulphur binding site	Binding Site

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.