2V1R

Yeast Pex13 SH3 domain complexed with a peptide from Pex14 at 2.1 A resolution

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
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d2v1rb_	All beta proteins	SH3-like barrel	SH3-domain	SH3-domain	automated matches	BAKER'S YEAST (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
A	d2v1ra_	All beta proteins	SH3-like barrel	SH3-domain	SH3-domain	automated matches	BAKER'S YEAST (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	SH3-domain	8037099	3000153	SCOP2B (2022-06-29)
A	SCOP2 Family	SH3-domain	8024720	4000369	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	SH3-domain	8037099	3000153	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	SH3_1	e2v1rB1	A: beta barrels	X: SH3	H: SH3	T: SH3	F: SH3_1	ECOD (1.6)
A	SH3_1	e2v1rA1	A: beta barrels	X: SH3	H: SH3	T: SH3	F: SH3_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.30.30.40	Mainly Beta	Roll	SH3 type barrels.	SH3 Domains	CATH (4.3.0)
A	2.30.30.40	Mainly Beta	Roll	SH3 type barrels.	SH3 Domains	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00018	SH3 domain (SH3_1)	SH3 domain	SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. First described in the Src cytoplasmic tyrosine kinase Swiss:P12931. The structure is a partly opened beta barrel.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PEROXISOMAL MEMBRANE PROTEIN PAS20	macromolecule transmembrane transporter activity protein transporter activity protein transmembrane transporter activity transporter activity transmembrane transporter activity protein-macromolecule adaptor activity molecular adaptor activity	protein localization cellular localization establishment of protein localization protein localization to peroxisome nitrogen compound transport protein transmembrane import into intracellular organelle transport peroxisomal membrane transport cellular component organization protein import into peroxisome matrix, docking localization peroxisome organization protein transmembrane transport establishment of localization in cell cellular macromolecule localization protein localization cellular localization establishment of protein localization protein localization to peroxisome nitrogen compound transport protein transmembrane import into intracellular organelle transport peroxisomal membrane transport cellular component organization protein import into peroxisome matrix, docking localization peroxisome organization protein transmembrane transport establishment of localization in cell cellular macromolecule localization cellular component organization or biogenesis establishment of protein localization to peroxisome intracellular protein transmembrane transport organic substance transport intracellular transport protein import into peroxisome matrix establishment of localization peroxisomal transport transmembrane transport organelle organization establishment of protein localization to organelle protein transport macromolecule localization protein localization to organelle cellular process intracellular protein transport	membrane-bounded organelle intracellular anatomical structure membrane peroxisome cellular anatomical entity intracellular membrane-bounded organelle microbody membrane intracellular organelle bounding membrane of organelle organelle peroxisomal membrane microbody cytoplasm organelle membrane membrane-bounded organelle intracellular anatomical structure membrane peroxisome cellular anatomical entity intracellular membrane-bounded organelle microbody membrane intracellular organelle bounding membrane of organelle organelle peroxisomal membrane microbody cytoplasm organelle membrane peroxisomal importomer complex protein-containing complex transporter complex
C [auth P], D [auth Q], E [auth R]	PEX14	protein binding binding signaling receptor binding macromolecule transmembrane transporter activity protein transporter activity protein transmembrane transporter activity transporter activity transmembrane transporter activity protein-macromolecule adaptor activity molecular adaptor activity	protein localization cellular localization establishment of protein localization protein localization to peroxisome nitrogen compound transport protein transmembrane import into intracellular organelle transport peroxisomal membrane transport cellular component organization protein import into peroxisome matrix, docking localization peroxisome organization protein transmembrane transport establishment of localization in cell cellular macromolecule localization protein localization cellular localization establishment of protein localization protein localization to peroxisome nitrogen compound transport protein transmembrane import into intracellular organelle transport peroxisomal membrane transport cellular component organization protein import into peroxisome matrix, docking localization peroxisome organization protein transmembrane transport establishment of localization in cell cellular macromolecule localization cellular component organization or biogenesis establishment of protein localization to peroxisome intracellular protein transmembrane transport organic substance transport intracellular transport protein import into peroxisome matrix establishment of localization peroxisomal transport transmembrane transport organelle organization establishment of protein localization to organelle protein transport macromolecule localization protein localization to organelle cellular process intracellular protein transport	membrane-bounded organelle intracellular anatomical structure membrane peroxisome cellular anatomical entity intracellular membrane-bounded organelle microbody membrane intracellular organelle bounding membrane of organelle organelle peroxisomal membrane microbody cytoplasm organelle membrane membrane-bounded organelle intracellular anatomical structure membrane peroxisome cellular anatomical entity intracellular membrane-bounded organelle microbody membrane intracellular organelle bounding membrane of organelle organelle peroxisomal membrane microbody cytoplasm organelle membrane peroxisomal importomer complex protein-containing complex transporter complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001452	SH3 domain	Domain
A, B	IPR036028	SH3-like domain superfamily	Homologous Superfamily
A, B	IPR007223	Peroxin 13, N-terminal	Domain
A, B	IPR035463	Peroxin 13	Family
C [auth P], D [auth Q], E [auth R]	IPR025655	Peroxisomal membrane protein 14	Family
C [auth P], D [auth Q], E [auth R]	IPR006785	Peroxisome membrane anchor protein Pex14p, N-terminal	Domain
C [auth P], D [auth Q], E [auth R]	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
C [auth P], D [auth Q], E [auth R]	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

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.