7LUB

Crystal structure of recombinant human fumarase in complex with D-2-amino-3-phosphono-propionic acid

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	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	0006525	biological_process	arginine metabolic process
A	0006974	biological_process	DNA damage response
A	0016829	molecular_function	lyase activity
A	0070062	cellular_component	extracellular exosome
A	0120162	biological_process	positive regulation of cold-induced thermogenesis
B	0000050	biological_process	urea cycle
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	0006525	biological_process	arginine metabolic process
B	0006974	biological_process	DNA damage response
B	0016829	molecular_function	lyase activity
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	14
Details	binding site for residue APO A 601

Chain	Residue
A	SER145
A	ASN373
A	GOL602
A	HOH722
B	THR234
B	HIS235
A	THR147
A	SER186
A	SER187
A	ASN188
A	SER365
A	ILE367
A	MET368
A	LYS371

---

site_id	AC2
Number of Residues	9
Details	binding site for residue GOL A 602

Chain	Residue
A	ASN150
A	MET151
A	ASN178
A	ASN182
A	SER187
A	SER365
A	SER366
A	ILE367
A	APO601

---

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL A 603

Chain	Residue
A	ALA295
A	LYS296
A	THR307
A	PRO309
A	HOH711
A	HOH720

---

site_id	AC4
Number of Residues	11
Details	binding site for residue GOL A 604

Chain	Residue
A	ARG261
A	ALA264
A	ALA265
A	GLU323
A	HOH706
A	HOH745
B	ARG261
B	ALA264
B	ALA265
B	GLU323
B	HOH769

---

site_id	AC5
Number of Residues	15
Details	binding site for residue APO B 601

Chain	Residue
A	THR234
A	HIS235
B	SER145
B	THR147
B	SER186
B	SER187
B	ASN188
B	SER365
B	ILE367
B	MET368
B	LYS371
B	ASN373
B	HOH709
B	HOH755
B	HOH795

---

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	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	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P9WN93","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"description":"in site B","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WN93","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	14
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by PRKDC","evidences":[{"source":"PubMed","id":"26237645","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---