3LIY

crystal structure of HTLV protease complexed with Statine-containing peptide inhibitor

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Acid proteases	8101693	3001059	SCOP2B (2022-06-29)
D [auth C]	SCOP2B Superfamily	Acid proteases	8101693	3001059	SCOP2B (2022-06-29)
G [auth E]	SCOP2B Superfamily	Acid proteases	8101693	3001059	SCOP2B (2022-06-29)
H [auth F]	SCOP2B Superfamily	Acid proteases	8101693	3001059	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Acid proteases	8101693	3001059	SCOP2B (2022-06-29)
E [auth D]	SCOP2B Superfamily	Acid proteases	8101693	3001059	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	RVP	e3liyA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: RVP	ECOD (1.6)
D [auth C]	RVP	e3liyC1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: RVP	ECOD (1.6)
G [auth E]	RVP	e3liyE1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: RVP	ECOD (1.6)
H [auth F]	RVP	e3liyF1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: RVP	ECOD (1.6)
B	RVP	e3liyB1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: RVP	ECOD (1.6)
E [auth D]	RVP	e3liyD1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: RVP	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.70.10	Mainly Beta	Beta Barrel	Cathepsin D, subunit A	domain 1	CATH (4.3.0)
D [auth C]	2.40.70.10	Mainly Beta	Beta Barrel	Cathepsin D, subunit A	domain 1	CATH (4.3.0)
G [auth E]	2.40.70.10	Mainly Beta	Beta Barrel	Cathepsin D, subunit A	domain 1	CATH (4.3.0)
H [auth F]	2.40.70.10	Mainly Beta	Beta Barrel	Cathepsin D, subunit A	domain 1	CATH (4.3.0)
B	2.40.70.10	Mainly Beta	Beta Barrel	Cathepsin D, subunit A	domain 1	CATH (4.3.0)
E [auth D]	2.40.70.10	Mainly Beta	Beta Barrel	Cathepsin D, subunit A	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, D [auth C], E [auth D], G [auth E], A, B, D [auth C], E [auth D], G [auth E], H [auth F]	PF00077	Retroviral aspartyl protease (RVP)	Retroviral aspartyl protease	Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a ...	Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (Pfam:PF00026).	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, D [auth C], E [auth D], G [auth E], A, B, D [auth C], E [auth D], G [auth E], H [auth F]	Protease	aspartic-type peptidase activity peptidase activity catalytic activity, acting on a protein hydrolase activity aspartic-type endopeptidase activity catalytic activity endopeptidase activity cation binding ion binding binding metal ion binding small molecule binding	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process	-
C [auth I], F [auth J], I [auth K]	statine-containing inhibitor	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, D [auth C], E [auth D], G [auth E], A, B, D [auth C], E [auth D], G [auth E], H [auth F]	IPR021109	Aspartic peptidase domain superfamily	Homologous Superfamily
A, B, D [auth C], E [auth D], G [auth E], A, B, D [auth C], E [auth D], G [auth E], H [auth F]	IPR001969	Aspartic peptidase, active site	Active Site
A, B, D [auth C], E [auth D], G [auth E], A, B, D [auth C], E [auth D], G [auth E], H [auth F]	IPR001995	Peptidase A2A, retrovirus, catalytic	Domain
A, B, D [auth C], E [auth D], G [auth E], A, B, D [auth C], E [auth D], G [auth E], H [auth F]	IPR018061	Retropepsins	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
C [auth I], F [auth J], I [auth K]	ACE	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 PSI-MOD : N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359
C [auth I], F [auth J], I [auth K]	STA	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354

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.