8F6N

Dihydropyrimidine Dehydrogenase (DPD) C671S Mutant Soaked with Thymine Quasi-Anaerobically

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0046872	molecular_function	metal ion binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050661	molecular_function	NADP binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0000166	molecular_function	nucleotide 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	0046872	molecular_function	metal ion binding
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0050661	molecular_function	NADP binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0000166	molecular_function	nucleotide 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	0046872	molecular_function	metal ion binding
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0050661	molecular_function	NADP binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	0000166	molecular_function	nucleotide 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	0046872	molecular_function	metal ion binding
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0050661	molecular_function	NADP binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding

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	MCSA1
Number of Residues	3
Details	M-CSA 800

Chain	Residue	Details
A	LYS574	electrostatic stabiliser
A	SER671	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	SER671	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	SER671	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	SER671	proton acceptor, proton donor
D	LYS709	electrostatic stabiliser

---