Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KAR

Crystal structure of FDTS (TM0449) mutant (H53D) with FAD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004799	molecular_function	thymidylate synthase activity
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	0032259	biological_process	methylation
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050797	molecular_function	thymidylate synthase (FAD) activity
A	0070402	molecular_function	NADPH binding
B	0004799	molecular_function	thymidylate synthase activity
B	0006231	biological_process	dTMP biosynthetic process
B	0006235	biological_process	dTTP biosynthetic process
B	0008168	molecular_function	methyltransferase activity
B	0009165	biological_process	nucleotide biosynthetic process
B	0032259	biological_process	methylation
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0050797	molecular_function	thymidylate synthase (FAD) activity
B	0070402	molecular_function	NADPH binding
C	0004799	molecular_function	thymidylate synthase activity
C	0006231	biological_process	dTMP biosynthetic process
C	0006235	biological_process	dTTP biosynthetic process
C	0008168	molecular_function	methyltransferase activity
C	0009165	biological_process	nucleotide biosynthetic process
C	0032259	biological_process	methylation
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0050797	molecular_function	thymidylate synthase (FAD) activity
C	0070402	molecular_function	NADPH binding
D	0004799	molecular_function	thymidylate synthase activity
D	0006231	biological_process	dTMP biosynthetic process
D	0006235	biological_process	dTTP biosynthetic process
D	0008168	molecular_function	methyltransferase activity
D	0009165	biological_process	nucleotide biosynthetic process
D	0032259	biological_process	methylation
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0050797	molecular_function	thymidylate synthase (FAD) activity
D	0070402	molecular_function	NADPH binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE FAD A 301

Chain	Residue
A	ARG78
C	GLU58
C	ILE81
C	ASN163
C	ARG165
C	FAD301
D	SER83
A	HIS79
A	ARG80
A	ILE81
A	ASN169
A	LEU173
A	ARG174
A	HOH420
A	HOH430

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE FAD B 301

Chain	Residue
B	ARG78
B	HIS79
B	ARG80
B	ILE81
B	ASN169
B	LEU173
B	ARG174
B	HOH408
B	HOH424
D	GLU58
D	ILE81
D	ASN163
D	ARG165
D	FAD301

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE FAD C 301

Chain	Residue
A	GLU58
A	ILE81
A	ASN163
A	ARG165
A	FAD301
B	SER83
C	ARG78
C	HIS79
C	ARG80
C	ILE81
C	ASN169
C	LEU173
C	HOH402
C	HOH417

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE FAD D 301

Chain	Residue
A	SER83
B	GLU58
B	ILE81
B	ASN163
B	ARG165
B	FAD301
D	ARG78
D	HIS79
D	ARG80
D	ILE81
D	ASN169
D	LEU173
D	HOH408
D	HOH413

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 2PE D 302

Chain	Residue
C	GLU203
C	LEU206
C	LEU215
C	LYS216
C	GLN219
D	HIS43
D	GLU46
D	TYR47
D	LYS50
D	HIS51

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Involved in ionization of N3 of dUMP, leading to its activation => ECO:0000269\|PubMed:27214228

Chain	Residue	Details
A	ARG174
B	ARG174
C	ARG174
D	ARG174

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:12791256, ECO:0000269\|PubMed:19370033, ECO:0000269\|PubMed:22477781, ECO:0000269\|PubMed:23019356, ECO:0000269\|PubMed:24563811, ECO:0000269\|PubMed:27214228, ECO:0000269\|PubMed:34315871, ECO:0007744\|PDB:1O26, ECO:0007744\|PDB:3G4A, ECO:0007744\|PDB:3N0B, ECO:0007744\|PDB:4GTD, ECO:0007744\|PDB:4KAS, ECO:0007744\|PDB:7NDW

Chain	Residue	Details
A	THR55
B	THR55
C	THR55
D	THR55

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:12791256, ECO:0000269\|PubMed:19370033, ECO:0000269\|PubMed:22477781, ECO:0000269\|PubMed:23019356, ECO:0000269\|PubMed:24563811, ECO:0000269\|PubMed:27214228, ECO:0007744\|PDB:1O26, ECO:0007744\|PDB:3G4A, ECO:0007744\|PDB:3N0B, ECO:0007744\|PDB:4GT9, ECO:0007744\|PDB:4KAS

Chain	Residue	Details
C	GLN75
C	ARG174
D	GLN75
D	ARG174
A	GLN75
A	ARG174
B	GLN75
B	ARG174

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:12211025, ECO:0000269\|PubMed:12791256, ECO:0000269\|PubMed:19370033, ECO:0000269\|PubMed:22477781, ECO:0000269\|PubMed:23019356, ECO:0000269\|PubMed:24563811, ECO:0000269\|PubMed:27214228, ECO:0000269\|PubMed:34315871, ECO:0007744\|PDB:1KQ4, ECO:0007744\|PDB:1O26, ECO:0007744\|PDB:3G4A, ECO:0007744\|PDB:3N0B, ECO:0007744\|PDB:4GTD, ECO:0007744\|PDB:4KAS, ECO:0007744\|PDB:7NDW

Chain	Residue	Details
B	ARG78
B	GLU86
B	ASN163
B	ASN169
C	ARG78
C	GLU86
C	ASN163
C	ASN169
D	ARG78
D	GLU86
D	ASN163
D	ASN169
A	ARG78
A	GLU86
A	ASN163
A	ASN169

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: in other chain => ECO:0000269\|PubMed:12791256, ECO:0000269\|PubMed:19370033, ECO:0000269\|PubMed:22477781, ECO:0000269\|PubMed:23019356, ECO:0000269\|PubMed:24563811, ECO:0000269\|PubMed:27214228, ECO:0007744\|PDB:1O26, ECO:0007744\|PDB:3G4A, ECO:0007744\|PDB:3N0B, ECO:0007744\|PDB:4GT9, ECO:0007744\|PDB:4KAS

Chain	Residue	Details
A	ARG147
B	ARG147
C	ARG147
D	ARG147

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)