4CCZ

Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0008705	molecular_function	methionine synthase activity
A	0009086	biological_process	methionine biosynthetic process
A	0031419	molecular_function	cobalamin binding
A	0042558	biological_process	pteridine-containing compound metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE THG A 1652

Chain	Residue
A	GLU376
A	SER578
A	ASN579
A	PHE582
A	ARG585
A	ARG591
A	ILE611
A	ASN379
A	GLY382
A	ARG384
A	ASP449
A	ASN470
A	MET498
A	ASP537
A	GLY576

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00333","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
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

---