4EIZ

Structure of Nb113 bound to apoDHFR

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
IMGT Antibody Annotation
SAbDab Antibody Annotation
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)
A	d4eiza_	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	Dihydrofolate reductases	Dihydrofolate reductase, prokaryotic type	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
B	d4eizb_	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	Dihydrofolate reductases	Dihydrofolate reductase, prokaryotic type	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
C	d4eizc1	All beta proteins	Immunoglobulin-like beta-sandwich	Immunoglobulin	V set domains (antibody variable domain-like)	automated matches	(Lama glama ) [TaxId: 9844 ],	SCOPe (2.08)
C	d4eizc2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Lama glama ) [TaxId: 9844 ],	SCOPe (2.08)
D	d4eizd1	All beta proteins	Immunoglobulin-like beta-sandwich	Immunoglobulin	V set domains (antibody variable domain-like)	automated matches	(Lama glama ) [TaxId: 9844 ],	SCOPe (2.08)
D	d4eizd2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Lama glama ) [TaxId: 9844 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Dihydrofolate reductase-like	8032695	3001255	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Dihydrofolate reductase-like	8032695	3001255	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	DHFR_1	e4eizA1	A: a/b three-layered sandwiches	X: Dihydrofolate reductases (From Topology)	H: Dihydrofolate reductases (From Topology)	T: Dihydrofolate reductases	F: DHFR_1	ECOD (1.6)
B	DHFR_1	e4eizB1	A: a/b three-layered sandwiches	X: Dihydrofolate reductases (From Topology)	H: Dihydrofolate reductases (From Topology)	T: Dihydrofolate reductases	F: DHFR_1	ECOD (1.6)
C	V-set_12	e4eizC1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: V-set_12	ECOD (1.6)
D	V-set_12	e4eizD1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: V-set_12	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.430.10	Alpha Beta	3-Layer(aba) Sandwich	Dihydrofolate Reductase, subunit A	Dihydrofolate Reductase, subunit A	CATH (4.3.0)
B	3.40.430.10	Alpha Beta	3-Layer(aba) Sandwich	Dihydrofolate Reductase, subunit A	Dihydrofolate Reductase, subunit A	CATH (4.3.0)
C	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
D	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)

IMGT Antibody Annotation IMGT Database Homepage

Chain	Protein Name	Description	Organism Name	Gene Allele Name(s)	Domain Name(s)	Receptor Type	Receptor Description	Provenance Source
C, D	Nb113	VH	Lama glama (llama)	IGHV3S301, IGHJ601	V-DOMAIN VH	IG	(VH)	IMGT (202415-0)

SAbDab Antibody Annotation SAbDab Database Homepage

Chain	Chain Class	Chain Subclass	Chain Type	Antigen Name(s)	Provenance Source
C, D	Heavy Chain	IGHV1	-	dihydrofolate reductase	SAbDab (2024-04-19)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00186	Dihydrofolate reductase (DHFR_1)	Dihydrofolate reductase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Dihydrofolate reductase	amide binding organic acid binding binding ion binding organic cyclic compound binding anion binding carboxylic acid binding heterocyclic compound binding methotrexate binding small molecule binding NADP+ binding nucleotide binding nucleoside phosphate binding purine nucleotide binding amide binding organic acid binding binding ion binding organic cyclic compound binding anion binding carboxylic acid binding heterocyclic compound binding methotrexate binding small molecule binding NADP+ binding nucleotide binding nucleoside phosphate binding purine nucleotide binding adenyl nucleotide binding NADP binding dihydrofolic acid binding modified amino acid binding NADPH binding vitamin binding folic acid binding dihydrofolate reductase activity oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-NH group of donors catalytic activity	response to stimulus response to chemical response to xenobiotic stimulus response to methotrexate response to organic substance response to organonitrogen compound response to oxygen-containing compound response to nitrogen compound response to organic cyclic compound cellular metabolic process small molecule metabolic process metabolic process cellular process one-carbon metabolic process response to stimulus response to chemical response to xenobiotic stimulus response to methotrexate response to organic substance response to organonitrogen compound response to oxygen-containing compound response to nitrogen compound response to organic cyclic compound cellular metabolic process small molecule metabolic process metabolic process cellular process one-carbon metabolic process organonitrogen compound metabolic process oxoacid metabolic process dicarboxylic acid metabolic process dihydrofolate metabolic process carboxylic acid metabolic process organic acid metabolic process cellular modified amino acid metabolic process organic cyclic compound metabolic process organic substance metabolic process folic acid-containing compound metabolic process pteridine-containing compound metabolic process vitamin metabolic process amide metabolic process water-soluble vitamin metabolic process folic acid metabolic process response to antibiotic folic acid-containing compound biosynthetic process organonitrogen compound biosynthetic process biosynthetic process cellular modified amino acid biosynthetic process organic cyclic compound biosynthetic process pteridine-containing compound biosynthetic process organic substance biosynthetic process tetrahydrofolate biosynthetic process tetrahydrofolate metabolic process serine family amino acid metabolic process cellular biosynthetic process amino acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process glycine metabolic process glycine biosynthetic process small molecule biosynthetic process L-amino acid biosynthetic process primary metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process proteinogenic amino acid biosynthetic process serine family amino acid biosynthetic process alpha-amino acid biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol
C, D	Nb113 Camel antibody fragment	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR017925	Dihydrofolate reductase conserved site	Conserved Site
A, B	IPR012259	Dihydrofolate reductase	Family
A, B	IPR024072	Dihydrofolate reductase-like domain superfamily	Homologous Superfamily
A, B	IPR001796	Dihydrofolate reductase domain	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.