Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1O25

Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with dUMP at 2.4 A resolution

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	10
Details	BINDING SITE FOR RESIDUE UMP A 603

Chain	Residue
A	GLU86
D	HOH437
A	LEU87
A	SER88
A	GLY89
A	ARG90
A	ARG147
D	GLN75
D	ARG78
D	ARG174

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE UMP B 608

Chain	Residue
B	GLU86
B	LEU87
B	SER88
B	GLY89
B	ARG90
B	ARG147
B	HOH347
C	GLN75
C	ARG78
C	ARG174
C	HOH326
C	HOH433

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE UMP C 613

Chain	Residue
B	GLN75
B	ARG78
B	ARG174
B	HOH346
C	PHE77
C	GLU86
C	LEU87
C	SER88
C	GLY89
C	ARG90
C	ARG147

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE UMP D 618

Chain	Residue
A	GLN75
A	ARG78
A	ARG174
A	HOH409
D	GLU86
D	LEU87
D	SER88
D	GLY89
D	ARG90
D	ARG147
D	HOH358
D	HOH434
D	HOH501

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
A	GLN75
A	ARG174
B	GLN75
B	ARG174
C	GLN75
C	ARG174
D	GLN75
D	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
A	ARG78
C	GLU86
C	ASN163
C	ASN169
D	ARG78
D	GLU86
D	ASN163
D	ASN169
A	GLU86
A	ASN163
A	ASN169
B	ARG78
B	GLU86
B	ASN163
B	ASN169
C	ARG78

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)