6U4O

Crystal structure of recombinant class II fumarase from Schistosoma mansoni

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000050	biological_process	urea cycle
A	0003824	molecular_function	catalytic activity
A	0004333	molecular_function	fumarate hydratase activity
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006099	biological_process	tricarboxylic acid cycle
A	0006106	biological_process	fumarate metabolic process
A	0006108	biological_process	malate metabolic process
A	0006525	biological_process	arginine metabolic process
A	0016829	molecular_function	lyase activity
A	0051289	biological_process	protein homotetramerization
B	0000050	biological_process	urea cycle
B	0003824	molecular_function	catalytic activity
B	0004333	molecular_function	fumarate hydratase activity
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006099	biological_process	tricarboxylic acid cycle
B	0006106	biological_process	fumarate metabolic process
B	0006108	biological_process	malate metabolic process
B	0006525	biological_process	arginine metabolic process
B	0016829	molecular_function	lyase activity
B	0051289	biological_process	protein homotetramerization
C	0000050	biological_process	urea cycle
C	0003824	molecular_function	catalytic activity
C	0004333	molecular_function	fumarate hydratase activity
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0006099	biological_process	tricarboxylic acid cycle
C	0006106	biological_process	fumarate metabolic process
C	0006108	biological_process	malate metabolic process
C	0006525	biological_process	arginine metabolic process
C	0016829	molecular_function	lyase activity
C	0051289	biological_process	protein homotetramerization
D	0000050	biological_process	urea cycle
D	0003824	molecular_function	catalytic activity
D	0004333	molecular_function	fumarate hydratase activity
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0006099	biological_process	tricarboxylic acid cycle
D	0006106	biological_process	fumarate metabolic process
D	0006108	biological_process	malate metabolic process
D	0006525	biological_process	arginine metabolic process
D	0016829	molecular_function	lyase activity
D	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue LMR C 501

Chain	Residue
C	SER105
D	ILE342
D	MET343
D	LYS346
D	ASN348
C	THR107
C	SER146
C	SER147
C	ASN148
C	THR194
C	HIS195
D	SER340
D	SER341

---

site_id	AC2
Number of Residues	5
Details	binding site for residue GOL C 502

Chain	Residue
C	ASN365
C	ASN390
C	HIS393
D	GLN361
D	HIS393

---

site_id	AC3
Number of Residues	8
Details	binding site for residue ACT C 503

Chain	Residue
C	SER300
C	ILE362
C	ASN365
C	HIS366
C	THR369
C	ASN390
C	LEU391
C	THR394

---

site_id	AC4
Number of Residues	14
Details	binding site for residue LMR A 501

Chain	Residue
A	SER105
A	THR107
A	SER146
A	SER147
A	ASN148
A	THR194
A	HIS195
B	GLY339
B	SER340
B	SER341
B	ILE342
B	MET343
B	LYS346
B	ASN348

---

site_id	AC5
Number of Residues	7
Details	binding site for residue GOL A 502

Chain	Residue
A	SER321
A	VAL332
A	LEU333
A	VAL347
A	ASN348
A	PRO349
B	GLN197

---

site_id	AC6
Number of Residues	5
Details	binding site for residue GOL A 503

Chain	Residue
A	ASN365
A	ASN390
A	HIS393
B	GLN361
B	HIS393

---

site_id	AC7
Number of Residues	8
Details	binding site for residue ACT A 504

Chain	Residue
A	SER300
A	ILE362
A	ASN365
A	HIS366
A	THR369
A	ASN390
A	LEU391
A	THR394

---

site_id	AC8
Number of Residues	14
Details	binding site for residue LMR D 501

Chain	Residue
C	GLY339
C	SER340
C	SER341
C	ILE342
C	MET343
C	LYS346
C	ASN348
D	SER105
D	THR107
D	SER146
D	SER147
D	ASN148
D	THR194
D	HIS195

---

site_id	AC9
Number of Residues	8
Details	binding site for residue ACT D 502

Chain	Residue
D	SER300
D	ILE362
D	ASN365
D	HIS366
D	THR369
D	ASN390
D	LEU391
D	THR394

---

site_id	AD1
Number of Residues	14
Details	binding site for residue LMR B 501

Chain	Residue
A	GLY339
A	SER340
A	SER341
A	ILE342
A	MET343
A	LYS346
A	ASN348
B	SER105
B	THR107
B	SER146
B	SER147
B	ASN148
B	THR194
B	HIS195

---

site_id	AD2
Number of Residues	6
Details	binding site for residue GOL B 502

Chain	Residue
B	VAL347
B	ASN348
B	PRO349
A	GLN197
B	SER321
B	LEU333

---

site_id	AD3
Number of Residues	8
Details	binding site for residue ACT B 503

Chain	Residue
B	SER300
B	ILE362
B	ASN365
B	HIS366
B	THR369
B	ASN390
B	LEU391
B	THR394

---

Functional Information from PROSITE/UniProt

site_id	PS00163
Number of Residues	10
Details	FUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN

Chain	Residue	Details
C	GLY339-ASN348

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P9WN93","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33549669","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6U4O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---