Annotations: 4PD0

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4pd0a3	All beta proteins	beta-clip	MoeA C-terminal domain-like	automated matches	automated matches	Rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
A	d4pd0a1	All beta proteins	MoeA N-terminal region -like	MoeA N-terminal region -like	MoeA N-terminal region -like	automated matches	Rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
A	d4pd0a2	Alpha and beta proteins (a/b)	Molybdenum cofactor biosynthesis proteins	Molybdenum cofactor biosynthesis proteins	automated matches	automated matches	Rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Molybdenum cofactor biosynthesis proteins	8041311	3000702	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	MoeA C-terminal domain-like	8041309	3000558	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	MoeA N-terminal region -like	8041310	3000572	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	MoeA_C	e4pd0A2	A: beta barrels	X: beta-clip	H: MoeA C-terminal domain-like (From Topology)	T: MoeA C-terminal domain-like	F: MoeA_C	ECOD (1.6)
A	MoeA_N_N	e4pd0A3	A: a+b two layers	X: MoeA-I/Ornithine decarboxylase-C/Reverse ferredoxin-like domain in RNA-polymerase (From Topology)	H: MoeA-I/Ornithine decarboxylase-C/Reverse ferredoxin-like domain in RNA-polymerase (From Topology)	T: MoeA-I/Ornithine decarboxylase-C/Reverse ferredoxin-like domain in RNA-polymerase	F: MoeA_N_N	ECOD (1.6)
A	MoeA_N_C	e4pd0A1	A: a+b complex topology	X: MoeA domain II (From Topology)	H: MoeA domain II (From Topology)	T: MoeA domain II	F: MoeA_N_C	ECOD (1.6)
A	MoCF_biosynth	e4pd0A4	A: a/b three-layered sandwiches	X: Molybdenum cofactor biosynthesis proteins (From Topology)	H: Molybdenum cofactor biosynthesis proteins (From Topology)	T: Molybdenum cofactor biosynthesis proteins	F: MoCF_biosynth	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.980.10	Alpha Beta	3-Layer(aba) Sandwich	Molybdenum Cofactor Biosythetic Enzyme	Chain A	CATH (4.3.0)
A	3.90.105.10	Alpha Beta	Alpha-Beta Complex	Molybdopterin biosynthesis moea protein, domain 2	Molybdopterin biosynthesis moea protein, domain 2	CATH (4.3.0)
A	2.170.190.11	Mainly Beta	Beta Complex	Molybdopterin biosynthesis moeA protein	domain 3	CATH (4.3.0)
A	2.40.340.10	Mainly Beta	Beta Barrel	Beta-clip	MoeA, C-terminal, domain IV	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF03454	MoeA C-terminal region (domain IV) (MoeA_C)	MoeA C-terminal region (domain IV)	This domain is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this domain is uncertain. The structure of this domain is known [1] and forms an incomplete beta barrel.	Domain
A	PF03453	MoeA N-terminal region (domain I and II) (MoeA_N)	MoeA N-terminal region (domain I and II)	-	Family
A	PF00994	Probable molybdopterin binding domain (MoCF_biosynth)	Probable molybdopterin binding domain	This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyr ...	This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Gephyrin	protein binding binding signaling receptor binding molybdopterin molybdotransferase activity transferase activity catalytic activity cytoskeletal protein binding tubulin binding protein-macromolecule adaptor activity molecular adaptor activity adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding protein binding binding signaling receptor binding molybdopterin molybdotransferase activity transferase activity catalytic activity cytoskeletal protein binding tubulin binding protein-macromolecule adaptor activity molecular adaptor activity 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 nitrate reductase activity oxidoreductase activity oxidoreductase activity, acting on other nitrogenous compounds as donors molybdopterin cofactor binding adenylyltransferase activity molybdopterin adenylyltransferase activity nucleotidyltransferase activity transferase activity, transferring phosphorus-containing groups cation binding metal ion binding identical protein binding	protein localization protein localization to postsynaptic specialization membrane cellular localization protein localization to postsynaptic membrane protein localization to cell periphery protein localization to synapse biological regulation localization within membrane protein localization to membrane protein-containing complex localization neurotransmitter receptor localization to postsynaptic specialization membrane localization regulation of postsynaptic membrane neurotransmitter receptor levels protein localization to organelle cellular macromolecule localization protein localization protein localization to postsynaptic specialization membrane cellular localization protein localization to postsynaptic membrane protein localization to cell periphery protein localization to synapse biological regulation localization within membrane protein localization to membrane protein-containing complex localization neurotransmitter receptor localization to postsynaptic specialization membrane localization regulation of postsynaptic membrane neurotransmitter receptor levels protein localization to organelle cellular macromolecule localization macromolecule localization cellular process protein localization to postsynapse regulation of biological quality protein localization to cell junction receptor localization to synapse membrane organization gamma-aminobutyric acid receptor clustering postsynapse organization neurotransmitter-gated ion channel clustering cellular component organization cell junction organization receptor clustering cellular component organization or biogenesis synapse organization postsynaptic membrane organization neurotransmitter receptor diffusion trapping receptor diffusion trapping postsynaptic neurotransmitter receptor diffusion trapping establishment of protein localization establishment of localization response to stimulus response to metal ion response to chemical glycine receptor clustering Mo-molybdopterin cofactor biosynthetic process Mo-molybdopterin cofactor metabolic process primary metabolic process prosthetic group metabolic process molybdopterin cofactor biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process molybdopterin cofactor metabolic process phosphate-containing compound metabolic process metabolic process protein metabolic process macromolecule metabolic process phosphorus metabolic process protein targeting developmental process multicellular organismal process nervous system development cellular component biogenesis multicellular organism development cellular component assembly cell junction assembly anatomical structure development synapse assembly system development neuromuscular junction development establishment of synaptic specificity at neuromuscular junction	cell periphery postsynapse cellular anatomical structure postsynaptic membrane synapse cell junction membrane plasma membrane plasma membrane region synaptic membrane intracellular anatomical structure cytoplasm cytosol glycinergic synapse cell periphery postsynapse cellular anatomical structure postsynaptic membrane synapse cell junction membrane plasma membrane plasma membrane region synaptic membrane intracellular anatomical structure cytoplasm cytosol glycinergic synapse postsynaptic specialization membrane postsynaptic specialization organelle somatodendritic compartment cell projection dendrite dendritic tree neuron projection plasma membrane bounded cell projection GABA-ergic synapse intracellular organelle cytoskeleton membraneless organelle intracellular membraneless organelle postsynaptic density neuron to neuron synapse asymmetric synapse cell body neuronal cell body postsynaptic specialization, intracellular component cytoplasmic side of plasma membrane cytoplasmic side of membrane side of membrane inhibitory synapse

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036688	MoeA, C-terminal, domain IV superfamily	Homologous Superfamily
A	IPR001453	MoaB/Mog domain	Domain
A	IPR005111	MoeA, C-terminal, domain IV	Domain
A	IPR036425	MoaB/Mog-like domain superfamily	Homologous Superfamily
A	IPR008284	Molybdenum cofactor biosynthesis, conserved site	Conserved Site
A	IPR005110	MoeA, N-terminal and linker domain	Domain
A	IPR038987	Molybdopterin biosynthesis protein MoeA-like	Family
A	IPR036135	MoeA, N-terminal and linker domain superfamily	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.