2GMJ

Structure of Porcine Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004174	molecular_function	electron-transferring-flavoprotein dehydrogenase activity
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0006979	biological_process	response to oxidative stress
A	0009055	molecular_function	electron transfer activity
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0022900	biological_process	electron transport chain
A	0022904	biological_process	respiratory electron transport chain
A	0046872	molecular_function	metal ion binding
A	0048039	molecular_function	ubiquinone binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0004174	molecular_function	electron-transferring-flavoprotein dehydrogenase activity
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0006979	biological_process	response to oxidative stress
B	0009055	molecular_function	electron transfer activity
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0022900	biological_process	electron transport chain
B	0022904	biological_process	respiratory electron transport chain
B	0046872	molecular_function	metal ion binding
B	0048039	molecular_function	ubiquinone binding
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 A 610

Chain	Residue
A	LEU504
A	CYS528
A	PRO529
A	CYS553
A	VAL554
A	CYS556
A	LYS557
A	CYS559
A	TRP570

---

site_id	AC2
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD A 611

Chain	Residue
A	GLY42
A	GLY44
A	PRO45
A	ALA46
A	GLU71
A	LYS72
A	HIS79
A	SER82
A	GLY83
A	ALA84
A	CYS85
A	ALA167
A	ALA212
A	GLU213
A	GLY214
A	HIS218
A	PHE275
A	LEU333
A	GLY353
A	CYS354
A	ILE364
A	LYS365
A	GLY366
A	THR367
A	HOH706
A	HOH719
A	HOH801

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B 612

Chain	Residue
B	LEU504
B	CYS528
B	PRO529
B	VAL532
B	CYS553
B	VAL554
B	CYS556
B	LYS557
B	CYS559

---

site_id	AC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE FAD B 613

Chain	Residue
B	GLY42
B	GLY44
B	PRO45
B	ALA46
B	GLU71
B	LYS72
B	HIS79
B	SER82
B	GLY83
B	ALA84
B	CYS85
B	ALA167
B	GLU213
B	GLY214
B	HIS218
B	PHE275
B	TYR277
B	ARG331
B	LEU333
B	GLY353
B	CYS354
B	ILE364
B	LYS365
B	GLY366
B	THR367
B	VAL572

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TBU A 621

Chain	Residue
A	ILE364
A	HOH788

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site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE TBU A 622

Chain	Residue
A	TYR271
A	THR438
A	TBU623

---

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TBU A 623

Chain	Residue
A	LEU131
A	TBU622

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site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TBU A 624

Chain	Residue
A	LYS324
A	LEU491

---

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE TBU B 625

Chain	Residue
B	TBU626

---

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TBU B 626

Chain	Residue
B	GLY273
B	TBU625

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	80
Details	INTRAMEM:

Chain	Residue	Details
A	LEU86-THR107
A	ASN405-SER424
B	LEU86-THR107
B	ASN405-SER424

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:17050691

Chain	Residue	Details
A	THR52
A	GLY282
A	GLU283
B	THR52
B	GLY282
B	GLU283

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	LEU538
A	ASP563
A	GLN566
A	ASN569
B	LEU538
B	ASP563
B	GLN566
B	ASN569

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7

Chain	Residue	Details
A	ALA73
A	VAL109
A	ARG200
A	ASN334
B	ALA73
B	VAL109
B	ARG200
B	ASN334

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16134

Chain	Residue	Details
A	CYS528
B	CYS528

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
A	THR80
A	CYS85

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

Chain	Residue	Details
B	THR80
B	CYS85

---

site_id	MCSA1
Number of Residues	7
Details	M-CSA 281

Chain	Residue	Details
A	GLU92	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	ILE341	activator, hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
A	ALA377	electrostatic stabiliser
A	LEU538	activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand
A	ASP563	activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand
A	GLN566	activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, metal ligand
A	ASN569	activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand

---

site_id	MCSA2
Number of Residues	7
Details	M-CSA 281

Chain	Residue	Details
B	GLU92	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
B	ILE341	activator, hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
B	ALA377	electrostatic stabiliser
B	LEU538	activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand
B	ASP563	activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand
B	GLN566	activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, metal ligand
B	ASN569	activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand

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