6F3M

Crystal structure of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa complexed with adenosine, K+ and Zn2+ cations

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	AdoHcyase_NAD	e6f3mA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: AdoHcyase_NAD	ECOD (1.6)
A	AdoHcyase	e6f3mA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: AdoHcyase	ECOD (1.6)
C	AdoHcyase_NAD	e6f3mC2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: AdoHcyase_NAD	ECOD (1.6)
C	AdoHcyase	e6f3mC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: AdoHcyase	ECOD (1.6)
D	AdoHcyase_NAD	e6f3mD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: AdoHcyase_NAD	ECOD (1.6)
D	AdoHcyase	e6f3mD2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: AdoHcyase	ECOD (1.6)
B	AdoHcyase_NAD	e6f3mB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: AdoHcyase_NAD	ECOD (1.6)
B	AdoHcyase	e6f3mB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: AdoHcyase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1480	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Adenosylhomocysteinase-like	CATH (utative)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)
C	3.40.50.1480	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Adenosylhomocysteinase-like	CATH (utative)
C	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)
D	3.40.50.1480	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Adenosylhomocysteinase-like	CATH (utative)
D	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)
B	3.40.50.1480	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Adenosylhomocysteinase-like	CATH (utative)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF05221	S-adenosyl-L-homocysteine hydrolase (AdoHcyase)	S-adenosyl-L-homocysteine hydrolase	-	Domain
A	PF00670	S-adenosyl-L-homocysteine hydrolase, NAD binding domain (AdoHcyase_NAD)	S-adenosyl-L-homocysteine hydrolase, NAD binding domain	-	Domain
B, C, D	PF05221	S-adenosyl-L-homocysteine hydrolase (AdoHcyase)	S-adenosyl-L-homocysteine hydrolase	-	Domain
B, C, D	PF00670	S-adenosyl-L-homocysteine hydrolase, NAD binding domain (AdoHcyase_NAD)	S-adenosyl-L-homocysteine hydrolase, NAD binding domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Adenosylhomocysteinase	hydrolase activity hydrolase activity, acting on carbon-sulfur bonds adenosylhomocysteinase activity catalytic activity	S-adenosylmethionine cycle S-adenosylmethionine metabolic process sulfur compound metabolic process metabolic process cellular process serine family amino acid metabolic process oxoacid metabolic process sulfur amino acid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process non-proteinogenic amino acid metabolic process S-adenosylmethionine cycle S-adenosylmethionine metabolic process sulfur compound metabolic process metabolic process cellular process serine family amino acid metabolic process oxoacid metabolic process sulfur amino acid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process non-proteinogenic amino acid metabolic process small molecule metabolic process non-proteinogenic amino acid biosynthetic process homocysteine metabolic process small molecule biosynthetic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process homocysteine biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process sulfur compound biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process serine family amino acid biosynthetic process L-homocysteine biosynthetic process sulfur amino acid biosynthetic process alpha-amino acid biosynthetic process one-carbon metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol
B, C, D	Adenosylhomocysteinase	hydrolase activity hydrolase activity, acting on carbon-sulfur bonds adenosylhomocysteinase activity catalytic activity	S-adenosylmethionine cycle S-adenosylmethionine metabolic process sulfur compound metabolic process metabolic process cellular process serine family amino acid metabolic process oxoacid metabolic process sulfur amino acid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process non-proteinogenic amino acid metabolic process S-adenosylmethionine cycle S-adenosylmethionine metabolic process sulfur compound metabolic process metabolic process cellular process serine family amino acid metabolic process oxoacid metabolic process sulfur amino acid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process non-proteinogenic amino acid metabolic process small molecule metabolic process non-proteinogenic amino acid biosynthetic process homocysteine metabolic process small molecule biosynthetic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process homocysteine biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process sulfur compound biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process serine family amino acid biosynthetic process L-homocysteine biosynthetic process sulfur amino acid biosynthetic process alpha-amino acid biosynthetic process one-carbon metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR015878	S-adenosyl-L-homocysteine hydrolase, NAD binding domain	Domain
A	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR020082	S-adenosyl-L-homocysteine hydrolase, conserved site	Conserved Site
A	IPR042172	Adenosylhomocysteinase-like superfamily	Homologous Superfamily
A	IPR000043	Adenosylhomocysteinase-like	Family
B, C, D	IPR015878	S-adenosyl-L-homocysteine hydrolase, NAD binding domain	Domain
B, C, D	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
B, C, D	IPR020082	S-adenosyl-L-homocysteine hydrolase, conserved site	Conserved Site
B, C, D	IPR042172	Adenosylhomocysteinase-like superfamily	Homologous Superfamily
B, C, D	IPR000043	Adenosylhomocysteinase-like	Family

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.