5A1I

The structure of Human MAT2A in complex with SAM, Adenosine, Methionine and PPNP.

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
Pharos: Disease Associations
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5a1ia1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	S-adenosylmethionine synthetase	8035289	3000766	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	S-adenosylmethionine synthetase	8035293	3000766	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	S-adenosylmethionine synthetase	8035292	3000766	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	S-AdoMet_synt_C	e5a1iA1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_C	ECOD (1.6)
A	S-AdoMet_synt_M	e5a1iA3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_M	ECOD (1.6)
A	S-AdoMet_synt_N	e5a1iA2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00438	S-adenosylmethionine synthetase, N-terminal domain (S-AdoMet_synt_N)	S-adenosylmethionine synthetase, N-terminal domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain
A	PF02773	S-adenosylmethionine synthetase, C-terminal domain (S-AdoMet_synt_C)	S-adenosylmethionine synthetase, C-terminal domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain
A	PF02772	S-adenosylmethionine synthetase, central domain (S-AdoMet_synt_M)	S-adenosylmethionine synthetase, central domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	S-ADENOSYLMETHIONINE SYNTHASE ISOFORM TYPE-2	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding methionine adenosyltransferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity cation binding metal ion binding identical protein binding protein binding	cellular response to stimulus positive regulation of cell communication regulation of cellular process positive regulation of signal transduction response to stimulus signaling positive regulation of biological process regulation of signal transduction positive regulation of TORC1 signaling intracellular signal transduction cell communication positive regulation of response to stimulus regulation of intracellular signal transduction positive regulation of TOR signaling cellular response to stimulus positive regulation of cell communication regulation of cellular process positive regulation of signal transduction response to stimulus signaling positive regulation of biological process regulation of signal transduction positive regulation of TORC1 signaling intracellular signal transduction cell communication positive regulation of response to stimulus regulation of intracellular signal transduction positive regulation of TOR signaling signal transduction regulation of TORC1 signaling positive regulation of cellular process TOR signaling regulation of biological process regulation of signaling regulation of TOR signaling biological regulation positive regulation of intracellular signal transduction regulation of response to stimulus regulation of cell communication cellular process TORC1 signaling positive regulation of signaling cellular response to methionine cellular response to acid chemical cellular response to nitrogen compound cellular response to amino acid stimulus response to nutrient levels response to nutrient response to oxygen-containing compound response to nitrogen compound response to amino acid cellular response to oxygen-containing compound cellular response to nutrient levels response to acid chemical cellular response to chemical stimulus response to methionine response to chemical cellular response to nutrient small molecule metabolic process metabolic process one-carbon metabolic process cellular component organization cellular component biogenesis protein hexamerization cellular component assembly protein-containing complex organization protein complex oligomerization protein-containing complex assembly cellular component organization or biogenesis sulfur compound biosynthetic process biosynthetic process S-adenosylmethionine biosynthetic process S-adenosylmethionine metabolic process sulfur compound metabolic process protein heterooligomerization response to peptide response to cytokine response to leukemia inhibitory factor cellular response to cytokine stimulus cellular response to leukemia inhibitory factor	protein-containing complex catalytic complex methionine adenosyltransferase complex transferase complex intracellular protein-containing complex cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR022636	S-adenosylmethionine synthetase superfamily	Homologous Superfamily
A	IPR022629	S-adenosylmethionine synthetase, central domain	Domain
A	IPR022628	S-adenosylmethionine synthetase, N-terminal	Domain
A	IPR022631	S-adenosylmethionine synthetase, conserved site	Conserved Site
A	IPR022630	S-adenosylmethionine synthetase, C-terminal	Domain
A	IPR002133	S-adenosylmethionine synthetase	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: P31153	oligodendroglioma pancreatic ductal adenocarcinoma progressive supranuclear palsy thoracic aortic aneurysm Alzheimer disease breast carcinoma Down syndrome IgA glomerulonephritis lymphoplasmacytic lymphoma malignant pancreatic neoplasm myocardial infarction osteosarcoma Pick disease prostate carcinoma astrocytic tumor oligodendroglioma pancreatic ductal adenocarcinoma progressive supranuclear palsy thoracic aortic aneurysm Alzheimer disease breast carcinoma Down syndrome IgA glomerulonephritis lymphoplasmacytic lymphoma malignant pancreatic neoplasm myocardial infarction osteosarcoma Pick disease prostate carcinoma astrocytic tumor chronic obstructive pulmonary disease glioblastoma large cell medulloblastoma malignant ependymoma Marfan syndrome non-small cell lung carcinoma ovarian carcinoma primitive neuroectodermal tumor sinusitis atypical teratoid rhabdoid tumor dermatomyositis heart disease lung adenocarcinoma malignant glioma medulloblastoma

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	methionine adenosyltransferase M-CSA #9	In biological systems, methyl groups are transferred from a small number of donors to a large number of acceptors. S-adenosylmethionine (AdoMet) is the most widespread of these donors, and is synthesised solely by the action of AdoMet synthase. The catalytic site of this enzyme, found in a cleft between two subunits, conducts an unusual reaction pathway where a triphosphate chain is cleaved from ATP as AdoMet is formed and the triphosphate is hydrolysed to diphosphate and phosphate before the product is released. There are three similar domains arranged around a pseudo-threefold symmetry axis.	Defined by 14 residues: HIS:A-29ASP:A-31LYS:A-32GLU:A-57GLU:A-70LYS:A-181PHE:A-250ASP:A-258ALA:A-259ARG:A-264LYS:A-265LYS:A-285LYS:A-289ASP:A-291 \| Explore in 3D: M-CSA Motif Definition Up to 10 residues are supported for Structure Motif searching, this motif has 14 residues. EC: 2.5.1.6 (PDB Primary Data)

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.