5UPP

Crystal structure of human fumarate hydratase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004333	molecular_function	fumarate hydratase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005694	cellular_component	chromosome
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
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	0006281	biological_process	DNA repair
A	0016829	molecular_function	lyase activity
A	0048873	biological_process	homeostasis of number of cells within a tissue
A	0070062	cellular_component	extracellular exosome
A	0120162	biological_process	positive regulation of cold-induced thermogenesis
B	0003824	molecular_function	catalytic activity
B	0004333	molecular_function	fumarate hydratase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005694	cellular_component	chromosome
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
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	0006281	biological_process	DNA repair
B	0016829	molecular_function	lyase activity
B	0048873	biological_process	homeostasis of number of cells within a tissue
B	0070062	cellular_component	extracellular exosome
B	0120162	biological_process	positive regulation of cold-induced thermogenesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue EPE A 601

Chain	Residue
A	ARG160
A	HOH754
A	GLU163
A	MET164
A	GLY166
A	PRO461
A	HIS462
A	ILE463
A	LYS467
A	HOH709

---

site_id	AC2
Number of Residues	7
Details	binding site for residue EPE B 601

Chain	Residue
B	ARG160
B	GLU163
B	MET164
B	PRO461
B	HIS462
B	LYS467
B	HOH769

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY364-ASN373

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P05042

Chain	Residue	Details
A	HIS235
B	HIS235

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P9WN93

Chain	Residue	Details
A	SER365
B	SER365

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P05042

Chain	Residue	Details
A	SER145
A	SER186
B	SER145
B	SER186

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: in site B => ECO:0000250|UniProtKB:P05042

Chain	Residue	Details
A	HIS176
B	HIS176

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P9WN93

Chain	Residue	Details
A	THR234
A	SER366
A	LYS371
B	THR234
B	SER366
B	LYS371

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P05042

Chain	Residue	Details
A	GLU378
B	GLU378

---

site_id	SWS_FT_FI7
Number of Residues	14
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P97807

Chain	Residue	Details
A	LYS61
B	LYS80
B	LYS115
B	LYS122
B	LYS223
B	LYS292
A	LYS66
A	LYS80
A	LYS115
A	LYS122
A	LYS223
A	LYS292
B	LYS61
B	LYS66

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P97807

Chain	Residue	Details
A	THR85
B	THR85

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR90
B	THR90

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS94
A	LYS256
B	LYS94
B	LYS256

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P97807

Chain	Residue	Details
A	LYS213
A	LYS502
B	LYS213
B	LYS502

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PRKDC => ECO:0000269|PubMed:26237645

Chain	Residue	Details
A	THR236
B	THR236

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER366
B	SER366

---

site_id	SWS_FT_FI14
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P97807

Chain	Residue	Details
A	LYS467
A	LYS473
B	LYS467
B	LYS473

---