Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SEJ

Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase from Cryptosporidium hominis Bound to 1843U89/NADPH/dUMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004146	molecular_function	dihydrofolate reductase activity
A	0004799	molecular_function	thymidylate synthase activity
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006231	biological_process	dTMP biosynthetic process
A	0006730	biological_process	one-carbon metabolic process
A	0008168	molecular_function	methyltransferase activity
A	0009165	biological_process	nucleotide biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016741	molecular_function	transferase activity, transferring one-carbon groups
A	0032259	biological_process	methylation
A	0046654	biological_process	tetrahydrofolate biosynthetic process
B	0000166	molecular_function	nucleotide binding
B	0004146	molecular_function	dihydrofolate reductase activity
B	0004799	molecular_function	thymidylate synthase activity
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006231	biological_process	dTMP biosynthetic process
B	0006730	biological_process	one-carbon metabolic process
B	0008168	molecular_function	methyltransferase activity
B	0009165	biological_process	nucleotide biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016741	molecular_function	transferase activity, transferring one-carbon groups
B	0032259	biological_process	methylation
B	0046654	biological_process	tetrahydrofolate biosynthetic process
C	0000166	molecular_function	nucleotide binding
C	0004146	molecular_function	dihydrofolate reductase activity
C	0004799	molecular_function	thymidylate synthase activity
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0006231	biological_process	dTMP biosynthetic process
C	0006730	biological_process	one-carbon metabolic process
C	0008168	molecular_function	methyltransferase activity
C	0009165	biological_process	nucleotide biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0016741	molecular_function	transferase activity, transferring one-carbon groups
C	0032259	biological_process	methylation
C	0046654	biological_process	tetrahydrofolate biosynthetic process
D	0000166	molecular_function	nucleotide binding
D	0004146	molecular_function	dihydrofolate reductase activity
D	0004799	molecular_function	thymidylate synthase activity
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0006231	biological_process	dTMP biosynthetic process
D	0006730	biological_process	one-carbon metabolic process
D	0008168	molecular_function	methyltransferase activity
D	0009165	biological_process	nucleotide biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0016741	molecular_function	transferase activity, transferring one-carbon groups
D	0032259	biological_process	methylation
D	0046654	biological_process	tetrahydrofolate biosynthetic process
E	0000166	molecular_function	nucleotide binding
E	0004146	molecular_function	dihydrofolate reductase activity
E	0004799	molecular_function	thymidylate synthase activity
E	0005739	cellular_component	mitochondrion
E	0005829	cellular_component	cytosol
E	0006231	biological_process	dTMP biosynthetic process
E	0006730	biological_process	one-carbon metabolic process
E	0008168	molecular_function	methyltransferase activity
E	0009165	biological_process	nucleotide biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0016741	molecular_function	transferase activity, transferring one-carbon groups
E	0032259	biological_process	methylation
E	0046654	biological_process	tetrahydrofolate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE UMP A 603

Chain	Residue
A	ARG257
A	ASN434
A	HIS464
A	TYR466
A	F89604
B	ARG382
B	ARG383
A	LEU399
A	CYS402
A	HIS403
A	GLN422
A	ARG423
A	SER424
A	CYS425
A	ASP426

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE F89 A 604

Chain	Residue
A	GLU294
A	ILE315
A	ASN319
A	ASP426
A	LEU429
A	GLY430
A	PHE433
A	TYR466
A	MET519
A	ALA520
A	UMP603
A	HOH633

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE F89 A 605

Chain	Residue
A	VAL9
A	VAL10
A	ALA11
A	LEU25
A	ASP32
A	LEU33
A	PHE36
A	SER37
A	ILE62
A	LEU67
A	ARG70
A	CYS113
A	THR134
A	NDP606
A	HOH669

site_id	AC4
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NDP A 606

Chain	Residue
A	VAL10
A	ALA11
A	ILE19
A	GLY20
A	ILE21
A	GLY23
A	GLN24
A	LEU25
A	GLY55
A	ARG56
A	LYS57
A	THR58
A	ILE75
A	SER76
A	SER77
A	SER78
A	ARG92
A	CYS113
A	GLY114
A	GLY115
A	GLU116
A	SER117
A	ILE118
A	TYR119
A	ASP121
A	THR145
A	F89605
A	HOH671
A	HOH675
A	HOH688

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE UMP B 607

Chain	Residue
A	ARG382
A	ARG383
B	ARG257
B	LEU399
B	CYS402
B	HIS403
B	GLN422
B	ARG423
B	SER424
B	ASP426
B	ASN434
B	HIS464
B	TYR466
B	F89608
B	HOH635
B	HOH711

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE F89 B 608

Chain	Residue
B	SER290
B	GLU294
B	ILE315
B	TRP316
B	ASN319
B	ASP426
B	GLY430
B	PHE433
B	MET519
B	ALA520
B	UMP607

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE F89 B 609

Chain	Residue
B	VAL9
B	VAL10
B	LEU25
B	ASP32
B	LEU33
B	PHE36
B	SER37
B	ILE62
B	LEU67
B	ARG70
B	CYS113
B	THR134
B	NDP610

site_id	AC8
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NDP B 610

Chain	Residue
B	VAL10
B	ALA11
B	ILE19
B	GLY20
B	ILE21
B	GLY23
B	GLN24
B	LEU25
B	GLY55
B	ARG56
B	LYS57
B	THR58
B	ILE75
B	SER76
B	SER77
B	SER78
B	ARG92
B	CYS113
B	GLY114
B	GLY115
B	GLU116
B	SER117
B	TYR119
B	ASP121
B	THR145
B	F89609
B	HOH649
B	HOH675

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE UMP C 611

Chain	Residue
C	ARG257
C	LEU399
C	CYS402
C	HIS403
C	GLN422
C	ARG423
C	SER424
C	ASP426
C	ASN434
C	HIS464
C	TYR466
C	F89612
C	HOH644
C	HOH688
D	ARG382
D	ARG383

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE F89 C 612

Chain	Residue
C	SER290
C	GLU294
C	ILE315
C	ASN319
C	ASP426
C	GLY430
C	PHE433
C	TYR466
C	MET519
C	ALA520
C	UMP611

site_id	BC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE F89 C 613

Chain	Residue
C	VAL9
C	VAL10
C	ALA11
C	LEU25
C	ASP32
C	LEU33
C	PHE36
C	SER37
C	ILE62
C	LEU67
C	ARG70
C	CYS113
C	THR134
C	NDP614
C	HOH643

site_id	BC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NDP C 614

Chain	Residue
C	VAL10
C	ALA11
C	ILE19
C	GLY20
C	GLY23
C	GLN24
C	LEU25
C	GLY55
C	ARG56
C	LYS57
C	THR58
C	ILE75
C	SER76
C	SER77
C	SER78
C	ARG92
C	CYS113
C	GLY114
C	GLY115
C	GLU116
C	SER117
C	TYR119
C	ASP121
C	THR145
C	F89613
C	HOH638

site_id	BC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE UMP D 615

Chain	Residue
C	ARG382
C	ARG383
D	ARG257
D	LEU399
D	CYS402
D	HIS403
D	GLN422
D	ARG423
D	SER424
D	ASP426
D	ASN434
D	HIS464
D	TYR466
D	F89616
D	HOH630

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE F89 D 616

Chain	Residue
D	GLU294
D	ILE315
D	ASN319
D	ASP426
D	GLY430
D	PHE433
D	TYR466
D	MET519
D	ALA520
D	UMP615

site_id	BC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE F89 D 617

Chain	Residue
D	VAL9
D	VAL10
D	ALA11
D	LEU25
D	ASP32
D	LEU33
D	PHE36
D	SER37
D	ILE62
D	LEU67
D	ARG70
D	CYS113
D	THR134
D	NDP618

site_id	BC7
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NDP D 618

Chain	Residue
D	VAL10
D	ALA11
D	ILE19
D	GLY20
D	GLY23
D	GLN24
D	LEU25
D	GLY55
D	ARG56
D	LYS57
D	THR58
D	ILE75
D	SER76
D	SER77
D	SER78
D	ARG92
D	CYS113
D	GLY114
D	GLY115
D	GLU116
D	SER117
D	ILE118
D	TYR119
D	ASP121
D	THR145
D	F89617
D	HOH662

site_id	BC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE UMP E 619

Chain	Residue
E	ARG257
E	ARG382
E	ARG383
E	LEU399
E	CYS402
E	HIS403
E	GLN422
E	ARG423
E	SER424
E	CYS425
E	ASP426
E	ASN434
E	HIS464
E	TYR466
E	F89620
E	HOH636

site_id	BC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE F89 E 620

Chain	Residue
E	GLU294
E	TYR314
E	ILE315
E	LEU399
E	ASP426
E	GLY430
E	PHE433
E	ALA520
E	UMP619
E	HOH636

site_id	CC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE F89 E 621

Chain	Residue
E	VAL9
E	VAL10
E	ALA11
E	LEU25
E	ASP32
E	LEU33
E	PHE36
E	SER37
E	ILE62
E	LEU67
E	ARG70
E	CYS113
E	THR134
E	NDP622

site_id	CC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NDP E 622

Chain	Residue
E	VAL10
E	ALA11
E	ILE19
E	GLY20
E	GLY23
E	GLN24
E	LEU25
E	GLY55
E	ARG56
E	LYS57
E	THR58
E	ILE75
E	SER76
E	SER77
E	SER78
E	ARG92
E	CYS113
E	GLY114
E	GLY115
E	GLU116
E	SER117
E	ILE118
E	TYR119
E	THR145
E	F89621

Functional Information from PROSITE/UniProt

site_id	PS00075
Number of Residues	23
Details	DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGingqLPWsise.DlkfFskiT

Chain	Residue	Details
A	GLY18-THR40

site_id	PS00091
Number of Residues	29
Details	THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrhIltaWNpsalsqma.....LpPCHvlsQYyV

Chain	Residue	Details
A	ARG382-VAL410

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1dhf

Chain	Residue	Details
A	ASP426
A	ASP462
A	GLU294
A	HIS464
A	SER424
A	CYS402

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhf

Chain	Residue	Details
E	LEU25
E	ASP32

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

Chain	Residue	Details
B	ASP426
B	ASP462
B	GLU294
B	HIS464
B	SER424
B	CYS402

site_id	CSA3
Number of Residues	6
Details	Annotated By Reference To The Literature 1dhf

Chain	Residue	Details
C	ASP426
C	ASP462
C	GLU294
C	HIS464
C	SER424
C	CYS402

site_id	CSA4
Number of Residues	6
Details	Annotated By Reference To The Literature 1dhf

Chain	Residue	Details
D	ASP426
D	ASP462
D	GLU294
D	HIS464
D	SER424
D	CYS402

site_id	CSA5
Number of Residues	6
Details	Annotated By Reference To The Literature 1dhf

Chain	Residue	Details
E	ASP426
E	ASP462
E	GLU294
E	HIS464
E	SER424
E	CYS402

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhf

Chain	Residue	Details
A	LEU25
A	ASP32

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhf

Chain	Residue	Details
B	LEU25
B	ASP32

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhf

Chain	Residue	Details
C	LEU25
C	ASP32

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhf

Chain	Residue	Details
D	LEU25
D	ASP32

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