2QD1

2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2qd1a_	Alpha and beta proteins (a/b)	Chelatase-like	Chelatase	Ferrochelatase	Ferrochelatase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d2qd1c_	Alpha and beta proteins (a/b)	Chelatase-like	Chelatase	Ferrochelatase	Ferrochelatase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d2qd1d_	Alpha and beta proteins (a/b)	Chelatase-like	Chelatase	Ferrochelatase	Ferrochelatase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2qd1b_	Alpha and beta proteins (a/b)	Chelatase-like	Chelatase	Ferrochelatase	Ferrochelatase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Chelatase	8042403	3001656	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Chelatase	8042403	3001656	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Chelatase	8042403	3001656	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Chelatase	8042403	3001656	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	Ferrochelatase	e2qd1A1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: Ferrochelatase	ECOD (1.6)
C	Ferrochelatase	e2qd1C1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: Ferrochelatase	ECOD (1.6)
D	Ferrochelatase	e2qd1D1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: Ferrochelatase	ECOD (1.6)
B	Ferrochelatase	e2qd1B1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: Ferrochelatase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1400	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
C	3.40.50.1400	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
D	3.40.50.1400	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.1400	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00762	Ferrochelatase (Ferrochelatase)	Ferrochelatase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Ferrochelatase	lyase activity ferrochelatase activity catalytic activity cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding RNA binding iron-responsive element binding organic cyclic compound binding lyase activity ferrochelatase activity catalytic activity cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding RNA binding iron-responsive element binding organic cyclic compound binding nucleic acid binding mRNA binding identical protein binding protein binding protein homodimerization activity protein dimerization activity iron-sulfur cluster binding 2 iron, 2 sulfur cluster binding metal cluster binding tetrapyrrole binding heme binding	response to stimulus response to chemical response to xenobiotic stimulus heme A biosynthetic process pigment metabolic process heme metabolic process porphyrin-containing compound biosynthetic process tetrapyrrole metabolic process heme biosynthetic process pigment biosynthetic process tetrapyrrole biosynthetic process biosynthetic process heme a metabolic process metabolic process response to stimulus response to chemical response to xenobiotic stimulus heme A biosynthetic process pigment metabolic process heme metabolic process porphyrin-containing compound biosynthetic process tetrapyrrole metabolic process heme biosynthetic process pigment biosynthetic process tetrapyrrole biosynthetic process biosynthetic process heme a metabolic process metabolic process cellular process porphyrin-containing compound metabolic process detection of light stimulus response to light stimulus detection of external stimulus response to external stimulus response to UV detection of abiotic stimulus detection of UV detection of stimulus response to abiotic stimulus response to radiation response to metal ion response to platinum ion response to methylmercury protoporphyrinogen IX metabolic process multicellular organismal-level iron ion homeostasis multicellular organismal process inorganic ion homeostasis multicellular organismal-level homeostasis chemical homeostasis homeostatic process multicellular organismal-level chemical homeostasis monoatomic ion homeostasis monoatomic cation homeostasis generation of precursor metabolites and energy organic hydroxy compound metabolic process sterol metabolic process steroid metabolic process cholesterol metabolic process alcohol metabolic process primary metabolic process secondary alcohol metabolic process small molecule metabolic process lipid metabolic process cellular response to stimulus response to ketone response to lipid cellular response to endogenous stimulus response to hormone response to steroid hormone cellular response to ketone cellular response to steroid hormone stimulus response to organic cyclic compound cellular response to hormone stimulus response to endogenous stimulus cellular response to dexamethasone stimulus response to glucocorticoid cellular response to organic cyclic compound cellular response to glucocorticoid stimulus response to oxygen-containing compound cellular response to oxygen-containing compound cellular response to corticosteroid stimulus response to corticosteroid cellular response to chemical stimulus cellular response to lipid response to dexamethasone response to alcohol response to ethanol response to lead ion response to insecticide response to toxic substance regulation of biosynthetic process regulation of biological process regulation of cellular process hemoglobin biosynthetic process regulation of protein metabolic process biological regulation regulation of macromolecule metabolic process macromolecule biosynthetic process regulation of primary metabolic process regulation of hemoglobin biosynthetic process regulation of macromolecule biosynthetic process protein metabolic process macromolecule metabolic process regulation of metabolic process hemoglobin metabolic process very-low-density lipoprotein particle assembly plasma lipoprotein particle organization protein-containing complex organization protein-lipid complex organization regulation of plasma lipoprotein particle levels cellular component organization cellular component biogenesis cellular component assembly protein-containing complex assembly plasma lipoprotein particle assembly protein-lipid complex assembly cellular component organization or biogenesis developmental process cellular developmental process hemopoiesis cell development erythrocyte differentiation myeloid cell differentiation immune system process cell differentiation anatomical structure development homeostasis of number of cells myeloid cell homeostasis erythrocyte homeostasis heme O metabolic process heme O biosynthetic process heme B biosynthetic process heme B metabolic process response to arsenic-containing substance	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope organelle membrane membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR019772	Ferrochelatase, active site	Active Site
A, B, C, D	IPR001015	Ferrochelatase	Family
A, B, C, D	IPR033644	Ferrochelatase, C-terminal	Domain
A, B, C, D	IPR033659	Ferrochelatase, N-terminal	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: P22830	erythropoietic protoporphyria protoporphyria, erythropoietic, 1 bile duct disease Fibrosis inherited porphyria psoriasis astrocytic tumor gallbladder disease lung cancer ovarian cancer pituitary cancer sarcoidosis autosomal erythropoietic protoporphyria cutaneous porphyria inborn errors of metabolism erythropoietic protoporphyria protoporphyria, erythropoietic, 1 bile duct disease Fibrosis inherited porphyria psoriasis astrocytic tumor gallbladder disease lung cancer ovarian cancer pituitary cancer sarcoidosis autosomal erythropoietic protoporphyria cutaneous porphyria inborn errors of metabolism medulloblastoma pancreatic ductal adenocarcinoma cystic fibrosis osteosarcoma Pick disease

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 R01GM157729.