3EHI

Crystal Structure of Human Thymidyalte Synthase M190K with Loop 181-197 stabilized in the inactive conformation

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0000900	molecular_function	mRNA regulatory element binding translation repressor activity
X	0004799	molecular_function	thymidylate synthase activity
X	0005542	molecular_function	folic acid binding
X	0005634	cellular_component	nucleus
X	0005737	cellular_component	cytoplasm
X	0005739	cellular_component	mitochondrion
X	0005743	cellular_component	mitochondrial inner membrane
X	0005759	cellular_component	mitochondrial matrix
X	0005829	cellular_component	cytosol
X	0006231	biological_process	dTMP biosynthetic process
X	0006235	biological_process	dTTP biosynthetic process
X	0008168	molecular_function	methyltransferase activity
X	0009165	biological_process	nucleotide biosynthetic process
X	0016020	cellular_component	membrane
X	0016740	molecular_function	transferase activity
X	0016741	molecular_function	transferase activity, transferring one-carbon groups
X	0017148	biological_process	negative regulation of translation
X	0032259	biological_process	methylation
X	0035999	biological_process	tetrahydrofolate interconversion
X	0046653	biological_process	tetrahydrofolate metabolic process
X	0071897	biological_process	DNA biosynthetic process
X	1990825	molecular_function	sequence-specific mRNA binding

Functional Information from PDB Data

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO X 318

Functional Information from PROSITE/UniProt

site_id	PS00091
Number of Residues	29
Details	THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImcaWNprdlplka.....LpPCHalcQFyV

Chain	Residue	Details
X	ARG175-VAL203

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P45352","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P45352","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1b02

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1b02