5XG3 | pdb_00005xg3

Crystal structure of the ATPgS-engaged Smc head domain with an extended coiled coil bound to the C-terminal domain of ScpA derived from Bacillus subtilis

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	SMC_N	e5xg3A2	A: alpha bundles	X: Helical domain in structural maintenance of chromosomes protein 3 (From Topology)	H: Helical domain in structural maintenance of chromosomes protein 3 (From Topology)	T: Helical domain in structural maintenance of chromosomes protein 3	F: SMC_N	ECOD (1.6)
A	SMC_N	e5xg3A1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: SMC_N	ECOD (1.6)
B	SMC_N_1	e5xg3B2	A: alpha bundles	X: Helical domain in structural maintenance of chromosomes protein 3 (From Topology)	H: Helical domain in structural maintenance of chromosomes protein 3 (From Topology)	T: Helical domain in structural maintenance of chromosomes protein 3	F: SMC_N_1	ECOD (1.6)
B	SMC_N	e5xg3B1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: SMC_N	ECOD (1.6)
C	SMC_ScpA_C	e5xg3C1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: SMC_ScpA_C	ECOD (1.6)
D	SMC_ScpA_C	e5xg3D1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: SMC_ScpA_C	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02463	RecF/RecN/SMC N terminal domain (SMC_N)	RecF/RecN/SMC N terminal domain	This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. Th ...	This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics [1]. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Chromosome partition protein Smc	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding DNA binding nucleic acid binding pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity ATP-dependent activity identical protein binding protein binding	nucleobase-containing compound metabolic process DNA replication metabolic process cellular process primary metabolic process DNA metabolic process macromolecule metabolic process nucleic acid metabolic process cell cycle chromosome segregation cell cycle process cellular component organization organelle organization chromosome condensation nucleobase-containing compound metabolic process DNA replication metabolic process cellular process primary metabolic process DNA metabolic process macromolecule metabolic process nucleic acid metabolic process cell cycle chromosome segregation cell cycle process cellular component organization organelle organization chromosome condensation chromosome organization cellular component organization or biogenesis sister chromatid cohesion	intracellular organelle cellular anatomical structure intracellular anatomical structure organelle membraneless organelle intracellular membraneless organelle chromosome cytoplasm
C, D	Segregation and condensation protein A	identical protein binding protein binding binding	nucleobase-containing compound metabolic process DNA replication metabolic process cellular process primary metabolic process DNA metabolic process macromolecule metabolic process nucleic acid metabolic process cell division cell cycle chromosome segregation cell cycle process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR010935	SMCs flexible hinge	Domain
A, B	IPR036277	SMCs flexible hinge superfamily	Homologous Superfamily
A, B	IPR003395	RecF/RecN/SMC, N-terminal	Domain
A, B	IPR024704	Structural maintenance of chromosomes protein	Family
A, B	IPR011890	Structural maintenance of chromosomes protein, prokaryotic	Family
A, B	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
C, D	IPR003768	Segregation and condensation protein A	Family
C, D	IPR023093	ScpA-like, C-terminal	Homologous Superfamily

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.