Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2GQ2

Mycobacterium tuberculosis ThyX-NADP complex

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	0016740	molecular_function	transferase activity
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	0016740	molecular_function	transferase activity
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	0016740	molecular_function	transferase activity
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	0016740	molecular_function	transferase activity
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	1
Details	BINDING SITE FOR RESIDUE IOD A 501

Chain	Residue
A	ARG115

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 502

Chain	Residue
A	ARG87
D	ARG87

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD D 503

Chain	Residue
A	ASN177
D	ARG87

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD D 505

Chain	Residue
D	THR239
D	GLU240
D	GOL408

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD D 507

Chain	Residue
D	VAL206

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IOD C 509

Chain	Residue
B	ASN177
C	ARG87
C	GLN106
C	ARG172

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD B 510

Chain	Residue
B	ARG87
B	ARG172

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD C 511

Chain	Residue
B	HIS98
C	HIS98

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD D 512

Chain	Residue
A	HIS98
A	HOH800

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD C 513

Chain	Residue
B	HOH690

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD D 514

Chain	Residue
A	ASP205

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 515

Chain	Residue
A	GLY121
A	VAL206

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K C 601

Chain	Residue
A	NAP300
B	NAP300
B	HOH628

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE K D 602

Chain	Residue
A	NAP300
B	NAP300

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K A 603

Chain	Residue
C	NAP300
D	NAP300
D	HOH687

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE K B 604

Chain	Residue
C	HOH610
D	NAP300

site_id	BC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAP A 300

Chain	Residue
A	TYR101
A	SER102
A	GLN103
A	SER105
A	HOH779
A	HOH787
A	HOH800
A	HOH806
B	NAP300
C	SER71
C	GLU74
C	HIS98
C	ASN188
C	ARG190
C	HIS194
C	K601
D	ARG95
D	HIS96
D	ARG97
D	HIS98
D	HIS194
D	ARG199
D	K602

site_id	BC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAP B 300

Chain	Residue
A	NAP300
A	HOH779
A	HOH806
B	GLN103
B	SER105
B	HOH628
B	HOH683
C	ARG95
C	HIS96
C	ARG97
C	HIS194
C	ARG199
C	K601
D	SER71
D	GLU74
D	HIS98
D	ASN188
D	ARG190
D	HIS194
D	K602
D	HOH634
D	HOH676

site_id	CC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAP C 300

Chain	Residue
C	HOH683
C	HOH684
D	NAP300
D	HOH642
A	SER71
A	GLU74
A	HIS98
A	ASN188
A	ARG190
A	HIS194
A	K603
A	PGE701
A	HOH785
B	ARG95
B	HIS96
B	ARG97
B	HIS194
B	ARG199
C	TYR101
C	SER102
C	GLN103
C	SER105
C	HOH610
C	HOH620
C	HOH635

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PGE A 701

Chain	Residue
A	TYR44
A	GLY68
A	HIS69
A	PHE70
A	SER71
A	HOH810
C	SER105
C	NAP300

site_id	CC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAP D 300

Chain	Residue
A	ARG95
A	HIS96
A	ARG97
A	HIS98
A	HIS194
A	ARG199
A	K603
B	SER71
B	GLU74
B	HIS98
B	ASN188
B	ARG190
B	HIS194
B	K604
B	HOH611
B	HOH680
C	NAP300
C	HOH635
D	TYR101
D	SER102
D	GLN103
D	SER105
D	HOH624
D	HOH642
D	HOH687

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 401

Chain	Residue
A	LYS14
A	THR15
A	GLY32
A	SER77
A	TYR189
A	VAL222
A	HOH766

site_id	CC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 402

Chain	Residue
B	LYS14
B	THR15
B	GLY31
B	GLY32
B	VAL78
B	TYR189
B	VAL222
B	HOH674

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 403

Chain	Residue
C	LYS14
C	THR15
C	GLY32
C	SER77
C	TYR189
C	VAL222

site_id	CC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 404

Chain	Residue
D	LYS14
D	THR15
D	GLY32
D	SER77
D	VAL78
D	TYR189
D	VAL222

site_id	CC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 405

Chain	Residue
B	TYR81
B	ARG182
D	ASP22
D	VAL23
D	PRO24
D	GLN45
D	TRP47

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 407

Chain	Residue
C	ILE213
C	GLU240
C	HOH658
C	HOH659

site_id	DC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 408

Chain	Residue
D	ARG210
D	THR239
D	GLU240
D	IOD505
D	HOH640

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Motif: {"description":"ThyX motif","evidences":[{"source":"HAMAP-Rule","id":"MF_01408","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Involved in ionization of N3 of dUMP, leading to its activation","evidences":[{"source":"HAMAP-Rule","id":"MF_01408","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	25
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16139296","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AF6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GWC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HZG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"16139296","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2AF6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16139296","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2AF6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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