3GTD

2.4 Angstrom crystal structure of fumarate hydratase from Rickettsia prowazekii

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	0016829	molecular_function	lyase activity
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	0016829	molecular_function	lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MLI A 462

Chain	Residue
A	SER98
A	THR100
A	ASN141
B	THR187
B	HIS188
B	MET321
B	LYS324
B	ASN326

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NA A 463

Chain	Residue
A	ASN343
A	HOH538
A	HOH546
B	GLN339
B	ASN343
B	HOH537
B	HOH542
A	GLN339

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MLI B 462

Chain	Residue
A	THR187
A	HIS188
A	GLY317
A	SER318
A	LYS324
A	ASN326
B	SER98
B	THR100
B	SER140
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

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	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:21904061, ECO:0007744|PDB:3GTD

Chain	Residue	Details
A	SER98
A	LYS324
B	SER98
B	LYS324

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: in site B => ECO:0000255|HAMAP-Rule:MF_00743

Chain	Residue	Details
A	HIS129
B	HIS129

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:21904061, ECO:0007744|PDB:3GTD

Chain	Residue	Details
A	SER139
B	SER139

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743

Chain	Residue	Details
A	THR187
A	SER319
B	THR187
B	SER319

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00743

Chain	Residue	Details
A	GLU331
B	GLU331

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
A	GLU331
A	SER318
A	LYS324

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
B	GLU331
B	LYS324

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
A	THR187
A	HIS188

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
B	THR187
B	HIS188

---

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

Chain	Residue	Details
A	GLU331
A	LYS324

---

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

Chain	Residue	Details
A	HIS188

---

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

Chain	Residue	Details
B	HIS188

---