2ONB

Human Thymidylate Synthase at low salt conditions with PDPA bound

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 316

Chain	Residue
A	ARG50
A	ARG78
A	ARG176
A	ARG185
A	LEU189
A	THR306

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 314

Chain	Residue
A	ILE227
A	HIS250
A	LEU252
A	GLN36
A	GLN62
A	ALA63

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site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 7PA A 319

Chain	Residue
A	ASP49
A	ARG50
A	THR51
A	ARG175
A	ASN183
A	ARG185
A	HIS196
A	ARG215
A	SER216
A	TYR258
A	HOH348

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG175-VAL203

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P0A884

Chain	Residue	Details
A	CME195

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: in other chain => ECO:0000250|UniProtKB:P0A884

Chain	Residue	Details
A	ARG50
A	ASN226

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P45352

Chain	Residue	Details
A	ARG175

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: in other chain => ECO:0000250|UniProtKB:P45352

Chain	Residue	Details
A	CME195
A	ARG215
A	HIS256

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P0A884

Chain	Residue	Details
A	ASP218
A	ALA312

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER114

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site_id	SWS_FT_FI7
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS287
A	LYS292
A	LYS308

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1lcb

Chain	Residue	Details
A	ASP254
A	SER216
A	ASP218
A	GLU87
A	HIS256

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