9SSR

Human Methionine Synthase With Methyltetrahydrofolate, Hydroxocobalamin, and SAM, N-Half From Full-Length

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000096	biological_process	sulfur amino acid metabolic process
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0007399	biological_process	nervous system development
A	0008168	molecular_function	methyltransferase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0008705	molecular_function	methionine synthase activity
A	0009086	biological_process	methionine biosynthetic process
A	0009235	biological_process	cobalamin metabolic process
A	0016740	molecular_function	transferase activity
A	0031103	biological_process	axon regeneration
A	0031419	molecular_function	cobalamin binding
A	0032259	biological_process	methylation
A	0046653	biological_process	tetrahydrofolate metabolic process
A	0046872	molecular_function	metal ion binding
A	0048678	biological_process	response to axon injury
A	0050667	biological_process	homocysteine metabolic process
A	0071267	biological_process	L-methionine salvage
A	0071732	biological_process	cellular response to nitric oxide

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	319
Details	Domain: {"description":"Hcy-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00333","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	261
Details	Domain: {"description":"Pterin-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00334","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00333","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2013","submissionDatabase":"PDB data bank","title":"Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains.","authors":["Vollmar M.","Kiyani W.","Krojer T.","Goubin S.","Burgess-Brown N.","Von Delft F.","Oppermann U.","Edwards A.","Arrowsmith C.","Bountra C.","Yue W.W."]}},{"source":"PDB","id":"4CCZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---