Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1H7W

Dihydropyrimidine dehydrogenase (DPD) from pig

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002058	molecular_function	uracil binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006210	biological_process	thymine catabolic process
A	0006212	biological_process	uracil catabolic process
A	0006214	biological_process	thymidine catabolic process
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0017113	molecular_function	dihydropyrimidine dehydrogenase (NADP+) activity
A	0019483	biological_process	beta-alanine biosynthetic process
A	0042803	molecular_function	protein homodimerization activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050661	molecular_function	NADP binding
A	0051536	molecular_function	iron-sulfur cluster binding
B	0002058	molecular_function	uracil binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006210	biological_process	thymine catabolic process
B	0006212	biological_process	uracil catabolic process
B	0006214	biological_process	thymidine catabolic process
B	0010181	molecular_function	FMN binding
B	0016491	molecular_function	oxidoreductase activity
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0017113	molecular_function	dihydropyrimidine dehydrogenase (NADP+) activity
B	0019483	biological_process	beta-alanine biosynthetic process
B	0042803	molecular_function	protein homodimerization activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0050661	molecular_function	NADP binding
B	0051536	molecular_function	iron-sulfur cluster binding
C	0002058	molecular_function	uracil binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006210	biological_process	thymine catabolic process
C	0006212	biological_process	uracil catabolic process
C	0006214	biological_process	thymidine catabolic process
C	0010181	molecular_function	FMN binding
C	0016491	molecular_function	oxidoreductase activity
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
C	0017113	molecular_function	dihydropyrimidine dehydrogenase (NADP+) activity
C	0019483	biological_process	beta-alanine biosynthetic process
C	0042803	molecular_function	protein homodimerization activity
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0050661	molecular_function	NADP binding
C	0051536	molecular_function	iron-sulfur cluster binding
D	0002058	molecular_function	uracil binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006210	biological_process	thymine catabolic process
D	0006212	biological_process	uracil catabolic process
D	0006214	biological_process	thymidine catabolic process
D	0010181	molecular_function	FMN binding
D	0016491	molecular_function	oxidoreductase activity
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0017113	molecular_function	dihydropyrimidine dehydrogenase (NADP+) activity
D	0019483	biological_process	beta-alanine biosynthetic process
D	0042803	molecular_function	protein homodimerization activity
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0050661	molecular_function	NADP binding
D	0051536	molecular_function	iron-sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 A1026

Chain	Residue
A	CYS91
A	PRO92
A	ILE97
A	ASN120
A	CYS130
A	CYS136
A	GLN156

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SF4 A1027

Chain	Residue
A	LYS81
A	CYS82
A	PRO86
A	CYS87
A	CYS140
A	ASN141
A	LEU142
A	ILE150
A	ILE152
A	CYS79
A	LEU80

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 A1028

Chain	Residue
A	ILE948
A	CYS953
A	ILE954
A	ASN955
A	CYS956
A	GLY957
A	CYS959
A	CYS996
A	PRO997
A	CYS1001

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 A1029

Chain	Residue
A	CYS963
A	TYR968
A	ILE971
A	CYS986
A	THR987
A	GLY988
A	CYS989
A	THR990
A	CYS992

site_id	AC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN A1030

Chain	Residue
A	ALA549
A	SER550
A	ALA551
A	LYS574
A	THR575
A	ILE590
A	ASN609
A	ASN668
A	LYS709
A	THR735
A	ASN736
A	SER766
A	GLY767
A	THR793
A	GLY794
A	GLY795
A	CYS816
A	SER817
A	GLN820
A	HOH2795
A	HOH2921
A	HOH3140

site_id	AC6
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD A1031

Chain	Residue
A	VAL129
A	GLY194
A	GLY196
A	PRO197
A	ALA198
A	GLU218
A	LYS219
A	GLN220
A	GLY225
A	LEU226
A	GLU230
A	ARG235
A	LYS259
A	SER260
A	LEU261
A	GLY282
A	ILE283
A	GLY284
A	LEU310
A	ASP342
A	THR343
A	ASP346
A	GLY480
A	ASP481
A	ASN487
A	THR488
A	THR489
A	SER492
A	HOH2373
A	HOH3141
A	HOH3142
A	HOH3143
A	HOH3144
A	HOH3145
A	HOH3146
A	HOH3147
A	HOH3148

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 B1026

Chain	Residue
B	ASN120
B	CYS130
B	CYS136
B	GLN156
B	CYS91
B	PRO92
B	ILE97

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SF4 B1027

Chain	Residue
B	CYS79
B	LEU80
B	LYS81
B	CYS82
B	PRO86
B	CYS87
B	CYS140
B	ASN141
B	LEU142
B	ILE150
B	ILE152

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 B1028

Chain	Residue
B	ILE948
B	CYS953
B	ILE954
B	CYS956
B	GLY957
B	CYS959
B	CYS996
B	PRO997
B	CYS1001
B	ILE1002

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 B1029

Chain	Residue
B	CYS963
B	TYR968
B	ILE971
B	VAL982
B	CYS986
B	THR987
B	GLY988
B	CYS989
B	THR990
B	CYS992

site_id	BC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN B1030

Chain	Residue
B	ALA549
B	SER550
B	ALA551
B	LYS574
B	THR575
B	ILE590
B	ASN609
B	ASN668
B	LYS709
B	THR735
B	ASN736
B	SER766
B	GLY767
B	THR793
B	GLY794
B	GLY795
B	CYS816
B	SER817
B	GLN820
B	HOH2815
B	HOH2917
B	HOH3117

site_id	BC3
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD B1031

Chain	Residue
B	VAL129
B	GLY194
B	GLY196
B	PRO197
B	ALA198
B	GLU218
B	LYS219
B	GLN220
B	GLY225
B	LEU226
B	GLU230
B	ARG235
B	LYS259
B	SER260
B	LEU261
B	GLY282
B	ILE283
B	GLY284
B	LEU310
B	THR343
B	ASP346
B	GLY480
B	ASP481
B	ASN487
B	THR488
B	THR489
B	SER492
B	HOH2367
B	HOH2370
B	HOH2640
B	HOH3119
B	HOH3120
B	HOH3121
B	HOH3122
B	HOH3123
B	HOH3124
B	HOH3125

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 C1026

Chain	Residue
C	CYS91
C	PRO92
C	ILE97
C	ASN120
C	CYS130
C	THR132
C	CYS136
C	GLN156

site_id	BC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SF4 C1027

Chain	Residue
C	CYS79
C	LEU80
C	LYS81
C	CYS82
C	PRO86
C	CYS87
C	CYS140
C	ASN141
C	LEU142
C	ILE150
C	ILE152

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 C1028

Chain	Residue
C	ILE948
C	CYS953
C	ILE954
C	CYS956
C	GLY957
C	CYS959
C	CYS996
C	PRO997
C	CYS1001
C	ILE1002

site_id	BC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 C1029

Chain	Residue
C	CYS963
C	TYR968
C	ILE971
C	VAL982
C	CYS986
C	THR987
C	GLY988
C	CYS989
C	THR990
C	CYS992

site_id	BC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN C1030

Chain	Residue
C	ALA549
C	SER550
C	ALA551
C	LYS574
C	THR575
C	ILE590
C	ASN609
C	ASN668
C	LYS709
C	THR735
C	ASN736
C	SER766
C	GLY767
C	THR793
C	GLY794
C	GLY795
C	CYS816
C	SER817
C	GLN820
C	HOH2838
C	HOH2926
C	HOH3169

site_id	BC9
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD C1031

Chain	Residue
C	VAL129
C	PRO131
C	GLY194
C	GLY196
C	PRO197
C	ALA198
C	GLU218
C	LYS219
C	GLN220
C	GLY225
C	LEU226
C	GLU230
C	ARG235
C	SER260
C	LEU261
C	GLY282
C	ILE283
C	GLY284
C	LEU310
C	ASP342
C	THR343
C	ASP346
C	GLY480
C	ASP481
C	ASN487
C	THR488
C	THR489
C	SER492
C	HOH2359
C	HOH2645
C	HOH3170
C	HOH3171
C	HOH3172
C	HOH3173
C	HOH3174
C	HOH3175
C	HOH3176

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 D1026

Chain	Residue
D	CYS91
D	PRO92
D	ILE97
D	ASN120
D	CYS130
D	THR132
D	CYS136
D	GLN156

site_id	CC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 D1027

Chain	Residue
D	CYS79
D	LEU80
D	LYS81
D	CYS82
D	CYS87
D	CYS140
D	ASN141
D	LEU142
D	ILE150
D	ILE152

site_id	CC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SF4 D1028

Chain	Residue
D	ILE948
D	CYS953
D	ILE954
D	CYS956
D	GLY957
D	LYS958
D	CYS959
D	CYS996
D	PRO997
D	CYS1001
D	ILE1002

site_id	CC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 D1029

Chain	Residue
D	CYS963
D	TYR968
D	ILE971
D	CYS986
D	THR987
D	GLY988
D	CYS989
D	THR990
D	CYS992

site_id	CC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN D1030

Chain	Residue
D	ALA549
D	SER550
D	ALA551
D	LYS574
D	THR575
D	ILE590
D	ASN609
D	ASN668
D	LYS709
D	THR735
D	ASN736
D	SER766
D	GLY767
D	THR793
D	GLY794
D	GLY795
D	CYS816
D	SER817
D	GLN820
D	HOH2847
D	HOH2994
D	HOH3182

site_id	CC6
Number of Residues	36
Details	BINDING SITE FOR RESIDUE FAD D1031

Chain	Residue
D	VAL129
D	GLY194
D	GLY196
D	PRO197
D	ALA198
D	GLU218
D	LYS219
D	GLN220
D	GLY225
D	LEU226
D	GLU230
D	ARG235
D	LYS259
D	SER260
D	LEU261
D	GLY282
D	ILE283
D	GLY284
D	LEU310
D	THR343
D	ASP346
D	GLY480
D	ASP481
D	ASN487
D	THR488
D	THR489
D	SER492
D	HOH2397
D	HOH2703
D	HOH3183
D	HOH3184
D	HOH3185
D	HOH3186
D	HOH3187
D	HOH3189
D	HOH3190

Functional Information from PROSITE/UniProt

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CtGCTlCLsVCP

Chain	Residue	Details
A	CYS986-PRO997

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	124
Details	Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	128
Details	Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	116
Details	Domain: {"description":"4Fe-4S ferredoxin-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11796730","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	80
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	176
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11796730","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q12882","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 2dor

Chain	Residue	Details
A	CYS671
A	LYS574

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 2dor

Chain	Residue	Details
B	CYS671
B	LYS574

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 2dor

Chain	Residue	Details
C	CYS671
C	LYS574

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 2dor

Chain	Residue	Details
D	CYS671
D	LYS574

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 2dor

Chain	Residue	Details
A	CYS671

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

Chain	Residue	Details
B	CYS671

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

Chain	Residue	Details
C	CYS671

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

Chain	Residue	Details
D	CYS671

site_id	MCSA1
Number of Residues	3
Details	M-CSA 800

Chain	Residue	Details
A	LYS574	electrostatic stabiliser
A	CYS671	proton acceptor, proton donor
A	LYS709	electrostatic stabiliser

site_id	MCSA2
Number of Residues	3
Details	M-CSA 800

Chain	Residue	Details
B	LYS574	electrostatic stabiliser
B	CYS671	proton acceptor, proton donor
B	LYS709	electrostatic stabiliser

site_id	MCSA3
Number of Residues	3
Details	M-CSA 800

Chain	Residue	Details
C	LYS574	electrostatic stabiliser
C	CYS671	proton acceptor, proton donor
C	LYS709	electrostatic stabiliser

site_id	MCSA4
Number of Residues	3
Details	M-CSA 800

Chain	Residue	Details
D	LYS574	electrostatic stabiliser
D	CYS671	proton acceptor, proton donor
D	LYS709	electrostatic stabiliser

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