4IUR

crystal structure of SHH1 SAWADEE domain in complex with H3K9me3 peptide

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 [auth B]	SCOP2B Superfamily	Tudor/PWWP/MBT domain-like	8092757	3000404	SCOP2B (2022-06-29)
A [auth B]	SCOP2B Superfamily	Tudor/PWWP/MBT domain-like	8092756	3000404	SCOP2B (2022-06-29)
C [auth A]	SCOP2B Superfamily	Tudor/PWWP/MBT domain-like	8092757	3000404	SCOP2B (2022-06-29)
C [auth A]	SCOP2B Superfamily	Tudor/PWWP/MBT domain-like	8092756	3000404	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 [auth B]	SAWADEE_C	e4iurB1	A: beta barrels	X: SH3	H: SH3	T: SH3	F: SAWADEE_C	ECOD (1.6)
A [auth B]	SAWADEE_N	e4iurB2	A: beta barrels	X: SH3	H: Chromo domain-like (From Topology)	T: Chromo domain-like	F: SAWADEE_N	ECOD (1.6)
C [auth A]	SAWADEE_C	e4iurA4	A: beta barrels	X: SH3	H: SH3	T: SH3	F: SAWADEE_C	ECOD (1.6)
C [auth A]	SAWADEE_N	e4iurA2	A: beta barrels	X: SH3	H: Chromo domain-like (From Topology)	T: Chromo domain-like	F: SAWADEE_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	2.40.50.40	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
A [auth B]	2.30.30.140	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)
C [auth A]	2.40.50.40	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
C [auth A]	2.30.30.140	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], C [auth A]	PF16719	SAWADEE domain (SAWADEE)	SAWADEE domain	The SAWADEE domain, found in plant homeobox proteins, has a pair of tandem tudor-like folds that bind chromatin [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], C [auth A]	SHH1 SAWADEE	chromatin binding binding cation binding ion binding metal ion binding small molecule binding	regulation of cellular process cellular biosynthetic process negative regulation of biological process negative regulation of cellular metabolic process negative regulation of cellular process negative regulation of macromolecule metabolic process regulation of biosynthetic process regulation of biological process cellular metabolic process negative regulation of metabolic process biological regulation regulation of cellular metabolic process regulation of macromolecule metabolic process gene expression regulation of cellular process cellular biosynthetic process negative regulation of biological process negative regulation of cellular metabolic process negative regulation of cellular process negative regulation of macromolecule metabolic process regulation of biosynthetic process regulation of biological process cellular metabolic process negative regulation of metabolic process biological regulation regulation of cellular metabolic process regulation of macromolecule metabolic process gene expression macromolecule biosynthetic process negative regulation of cellular biosynthetic process regulatory ncRNA-mediated gene silencing regulation of cellular biosynthetic process regulation of gene expression negative regulation of gene expression biosynthetic process negative regulation of biosynthetic process negative regulation of macromolecule biosynthetic process regulation of macromolecule biosynthetic process metabolic process cellular process macromolecule metabolic process regulation of metabolic process cellular component organization chromatin organization DNA methylation-dependent heterochromatin formation chromatin remodeling cellular component organization or biogenesis heterochromatin formation epigenetic regulation of gene expression constitutive heterochromatin formation negative regulation of gene expression, epigenetic	membrane-bounded organelle intracellular organelle intracellular anatomical structure organelle nucleus intracellular membrane-bounded organelle cellular anatomical entity
B [auth C]	Histone H3.2, H3(1-15)K9me3	DNA binding binding organic cyclic compound binding nucleic acid binding protein heterodimerization activity protein binding protein dimerization activity structural molecule activity structural constituent of chromatin	-	membrane-bounded organelle intracellular organelle intracellular anatomical structure plastid organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle extracellular region intracellular non-membrane-bounded organelle non-membrane-bounded organelle chromocenter cytosol cell periphery membrane-bounded organelle intracellular organelle intracellular anatomical structure plastid organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle extracellular region intracellular non-membrane-bounded organelle non-membrane-bounded organelle chromocenter cytosol cell periphery plasma membrane membrane protein-containing complex protein-DNA complex nucleosome chromatin chromosome nucleus

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], C [auth A]	IPR032001	SAWADEE domain	Domain
A [auth B], C [auth A]	IPR039276	Protein SAWADEE HOMEODOMAIN HOMOLOG 1/2	Family
B [auth C]	IPR009072	Histone-fold	Homologous Superfamily
B [auth C]	IPR007125	Histone H2A/H2B/H3	Domain
B [auth C]	IPR000164	Histone H3/CENP-A	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
B [auth C]	M3L	Parent Component: LYS RESID: AA0074 PSI-MOD : N6,N6,N6-trimethyl-L-lysine MOD:00083

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.