1TJW

Crystal Structure of T161D Duck Delta 2 Crystallin Mutant with bound argininosuccinate

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)
A	d1tjwa_	All alpha proteins	L-aspartase-like	L-aspartase-like	L-aspartase/fumarase	Argininosuccinate lyase/delta-crystallin	(Anas platyrhynchos ) [TaxId: 8839 ],	SCOPe (2.08)
B	d1tjwb_	All alpha proteins	L-aspartase-like	L-aspartase-like	L-aspartase/fumarase	Argininosuccinate lyase/delta-crystallin	(Anas platyrhynchos ) [TaxId: 8839 ],	SCOPe (2.08)
C	d1tjwc_	All alpha proteins	L-aspartase-like	L-aspartase-like	L-aspartase/fumarase	Argininosuccinate lyase/delta-crystallin	(Anas platyrhynchos ) [TaxId: 8839 ],	SCOPe (2.08)
D	d1tjwd_	All alpha proteins	L-aspartase-like	L-aspartase-like	L-aspartase/fumarase	Argininosuccinate lyase/delta-crystallin	(Anas platyrhynchos ) [TaxId: 8839 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	L-aspartase-like	8040249	3001572	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	L-aspartase-like	8040249	3001572	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	L-aspartase-like	8040249	3001572	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	L-aspartase-like	8040249	3001572	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	Lyase_1_N	e1tjwA3	A: alpha arrays	X: L-aspartase N-terminal domain-like (From Topology)	H: L-aspartase N-terminal domain-like (From Topology)	T: L-aspartase N-terminal domain-like	F: Lyase_1_N	ECOD (1.6)
A	ASL_C2	e1tjwA2	A: alpha arrays	X: L-aspartase C-terminal domain-like (From Homology)	H: L-aspartase C-terminal domain-like	T: L-aspartase C-terminal domain-like	F: ASL_C2	ECOD (1.6)
A	Lyase_1_C	e1tjwA4	A: alpha arrays	X: L-aspartase middle domain-like	H: L-aspartase middle domain-like (From Topology)	T: L-aspartase middle domain-like	F: Lyase_1_C	ECOD (1.6)
B	Lyase_1_N	e1tjwB3	A: alpha arrays	X: L-aspartase N-terminal domain-like (From Topology)	H: L-aspartase N-terminal domain-like (From Topology)	T: L-aspartase N-terminal domain-like	F: Lyase_1_N	ECOD (1.6)
B	ASL_C2	e1tjwB2	A: alpha arrays	X: L-aspartase C-terminal domain-like (From Homology)	H: L-aspartase C-terminal domain-like	T: L-aspartase C-terminal domain-like	F: ASL_C2	ECOD (1.6)
B	Lyase_1_C	e1tjwB4	A: alpha arrays	X: L-aspartase middle domain-like	H: L-aspartase middle domain-like (From Topology)	T: L-aspartase middle domain-like	F: Lyase_1_C	ECOD (1.6)
C	Lyase_1_N	e1tjwC3	A: alpha arrays	X: L-aspartase N-terminal domain-like (From Topology)	H: L-aspartase N-terminal domain-like (From Topology)	T: L-aspartase N-terminal domain-like	F: Lyase_1_N	ECOD (1.6)
C	ASL_C2	e1tjwC2	A: alpha arrays	X: L-aspartase C-terminal domain-like (From Homology)	H: L-aspartase C-terminal domain-like	T: L-aspartase C-terminal domain-like	F: ASL_C2	ECOD (1.6)
C	Lyase_1_C	e1tjwC4	A: alpha arrays	X: L-aspartase middle domain-like	H: L-aspartase middle domain-like (From Topology)	T: L-aspartase middle domain-like	F: Lyase_1_C	ECOD (1.6)
D	Lyase_1_N	e1tjwD3	A: alpha arrays	X: L-aspartase N-terminal domain-like (From Topology)	H: L-aspartase N-terminal domain-like (From Topology)	T: L-aspartase N-terminal domain-like	F: Lyase_1_N	ECOD (1.6)
D	ASL_C2	e1tjwD2	A: alpha arrays	X: L-aspartase C-terminal domain-like (From Homology)	H: L-aspartase C-terminal domain-like	T: L-aspartase C-terminal domain-like	F: ASL_C2	ECOD (1.6)
D	Lyase_1_C	e1tjwD4	A: alpha arrays	X: L-aspartase middle domain-like	H: L-aspartase middle domain-like (From Topology)	T: L-aspartase middle domain-like	F: Lyase_1_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.275.10	Mainly Alpha	Orthogonal Bundle	Fumarase C	Chain B, domain 1	CATH (4.3.0)
A	1.20.200.10	Mainly Alpha	Up-down Bundle	Fumarase C	Chain A, domain 2	CATH (4.3.0)
A	1.10.40.30	Mainly Alpha	Orthogonal Bundle	Ribonucleotide Reductase Protein R1	domain 1	CATH (4.3.0)
B	1.10.275.10	Mainly Alpha	Orthogonal Bundle	Fumarase C	Chain B, domain 1	CATH (4.3.0)
B	1.20.200.10	Mainly Alpha	Up-down Bundle	Fumarase C	Chain A, domain 2	CATH (4.3.0)
B	1.10.40.30	Mainly Alpha	Orthogonal Bundle	Ribonucleotide Reductase Protein R1	domain 1	CATH (4.3.0)
C	1.10.275.10	Mainly Alpha	Orthogonal Bundle	Fumarase C	Chain B, domain 1	CATH (4.3.0)
C	1.20.200.10	Mainly Alpha	Up-down Bundle	Fumarase C	Chain A, domain 2	CATH (4.3.0)
C	1.10.40.30	Mainly Alpha	Orthogonal Bundle	Ribonucleotide Reductase Protein R1	domain 1	CATH (4.3.0)
D	1.10.275.10	Mainly Alpha	Orthogonal Bundle	Fumarase C	Chain B, domain 1	CATH (4.3.0)
D	1.20.200.10	Mainly Alpha	Up-down Bundle	Fumarase C	Chain A, domain 2	CATH (4.3.0)
D	1.10.40.30	Mainly Alpha	Orthogonal Bundle	Ribonucleotide Reductase Protein R1	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF14698	Argininosuccinate lyase C-terminal (ASL_C2)	Argininosuccinate lyase C-terminal	This domain is found at the C-terminus of argininosuccinate lyase [1-2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Delta crystallin II	amidine-lyase activity argininosuccinate lyase activity lyase activity catalytic activity carbon-nitrogen lyase activity structural molecule activity structural constituent of eye lens	L-arginine biosynthetic process oxoacid metabolic process glutamine family amino acid biosynthetic process cellular biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process glutamine family amino acid metabolic process arginine metabolic process small molecule metabolic process small molecule biosynthetic process cellular metabolic process L-arginine biosynthetic process oxoacid metabolic process glutamine family amino acid biosynthetic process cellular biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process glutamine family amino acid metabolic process arginine metabolic process small molecule metabolic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process alpha-amino acid biosynthetic process ornithine metabolic process arginine biosynthetic process via ornithine non-proteinogenic amino acid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR000362	Fumarate lyase family	Family
A, B, C, D	IPR009049	Argininosuccinate lyase	Family
A, B, C, D	IPR022761	Fumarate lyase, N-terminal	Domain
A, B, C, D	IPR024083	Fumarase/histidase, N-terminal	Homologous Superfamily
A, B, C, D	IPR008948	L-Aspartase-like	Homologous Superfamily
A, B, C, D	IPR020557	Fumarate lyase, conserved site	Conserved Site
A, B, C, D	IPR029419	Argininosuccinate lyase, C-terminal	Domain

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.