2FUS

MUTATIONS OF FUMARASE THAT DISTINGUISH BETWEEN THE ACTIVE SITE AND A NEARBY DICARBOXYLIC ACID BINDING SITE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004333	molecular_function	fumarate hydratase activity
A	0005737	cellular_component	cytoplasm
A	0006099	biological_process	tricarboxylic acid cycle
A	0006106	biological_process	fumarate metabolic process
A	0006108	biological_process	malate metabolic process
A	0006979	biological_process	response to oxidative stress
A	0016829	molecular_function	lyase activity
A	0042802	molecular_function	identical protein binding
B	0003824	molecular_function	catalytic activity
B	0004333	molecular_function	fumarate hydratase activity
B	0005737	cellular_component	cytoplasm
B	0006099	biological_process	tricarboxylic acid cycle
B	0006106	biological_process	fumarate metabolic process
B	0006108	biological_process	malate metabolic process
B	0006979	biological_process	response to oxidative stress
B	0016829	molecular_function	lyase activity
B	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CIT A 468

Chain	Residue
A	HOH505
A	HOH654
B	THR187
B	HIS188
A	THR100
A	SER139
A	SER140
A	ASN141
A	LYS324
A	ASN326

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CIT B 468

Chain	Residue
A	THR187
A	HIS188
B	THR100
B	SER139
B	SER140
B	ASN141
B	LYS324
B	ASN326
B	HOH481

---

site_id	S1
Number of Residues	3
Details	THE ACTIVE SITE IS GENERATED FROM THREE OF THE FOUR SUBUNITS WITHIN THE TETRAMER. THE ENTRY CONTAINS CHAINS A AND B. CHAINS C AND D CAN BE GENERATED FROM CHAINS A AND B. THE ACTIVE SITE CONTAINS RESIDUES FROM CHAINS B, C, AND D. BECAUSE OF PDB FORMAT RESTRICTIONS, ONLY THE RESIDUES FROM CHAIN B ARE LISTED ON THE SITE RECORD BELOW. THE FOLLOWING RESIDUES ARE ALSO PART OF THE ACTIVE SITE: LYS C 324 ASN C 326 GLU C 331 ASN D 188

Chain	Residue
B	SER98
B	THR100
B	ASN141

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY317-ASN326

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:9098893

Chain	Residue	Details
A	HIS188
B	HIS188

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00743

Chain	Residue	Details
A	SER318
B	SER318

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:12021453, ECO:0000305|PubMed:8909293, ECO:0000305|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS

Chain	Residue	Details
A	SER98
B	SER98

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR

Chain	Residue	Details
A	ARG126
B	ARG126

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: in site B => ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR, ECO:0007744|PDB:1KQ7

Chain	Residue	Details
A	ASN129
B	ASN129

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS

Chain	Residue	Details
A	SER139
B	SER139

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743

Chain	Residue	Details
A	THR187
A	SER319
A	LYS324
B	THR187
B	SER319
B	LYS324

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:8909293

Chain	Residue	Details
A	GLU331
B	GLU331

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
A	THR187
A	HIS188
B	GLU331
B	LYS324

---

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
A	GLU331
A	SER318
A	LYS324
B	THR187
B	HIS188

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 569

Chain	Residue	Details
A	HIS188	electrostatic stabiliser, proton acceptor
A	SER318	proton donor
A	LYS324	electrostatic stabiliser
A	GLU331	increase basicity

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 569

Chain	Residue	Details
B	HIS188	electrostatic stabiliser, proton acceptor
B	SER318	proton donor
B	LYS324	electrostatic stabiliser
B	GLU331	increase basicity

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