3QJT

The structure of and photolytic induced changes of carbon monoxide binding to the cytochrome ba3-oxidase from Thermus thermophilus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004129	molecular_function	cytochrome-c oxidase activity
A	0005886	cellular_component	plasma membrane
A	0006119	biological_process	oxidative phosphorylation
A	0006811	biological_process	monoatomic ion transport
A	0009060	biological_process	aerobic respiration
A	0016020	cellular_component	membrane
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
A	0070469	cellular_component	respirasome
A	1902600	biological_process	proton transmembrane transport
B	0004129	molecular_function	cytochrome-c oxidase activity
B	0005507	molecular_function	copper ion binding
B	0005886	cellular_component	plasma membrane
B	0016020	cellular_component	membrane
B	0046872	molecular_function	metal ion binding
B	0070469	cellular_component	respirasome
B	1902600	biological_process	proton transmembrane transport
C	0004129	molecular_function	cytochrome-c oxidase activity
C	0005886	cellular_component	plasma membrane
C	0006811	biological_process	monoatomic ion transport
C	0016020	cellular_component	membrane
C	0070469	cellular_component	respirasome
C	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU1 A 803

Chain	Residue
A	HIS233
A	HIS282
A	HIS283
A	CMO563

---

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM A 800

Chain	Residue
A	TYR65
A	LEU69
A	HIS72
A	ASN76
A	ALA77
A	TYR133
A	PHE385
A	HIS386
A	VAL389
A	ALA390
A	THR394
A	TRP428
A	MET432
A	MET435
A	ARG449
A	ARG450
A	ALA451
A	LEU477
A	SER36
A	GLY39
A	PRO40
A	GLN42
A	TYR46

---

site_id	AC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HAS A 801

Chain	Residue
A	TYR133
A	VAL236
A	TYR237
A	TRP239
A	HIS282
A	THR302
A	SER309
A	LEU310
A	ALA313
A	LEU320
A	VAL350
A	LEU353
A	PHE356
A	GLY363
A	ASN366
A	ALA367
A	ASP372
A	HIS376
A	VAL381
A	HIS384
A	PHE385
A	GLN388
A	VAL389
A	ARG449
A	CMO563

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CUA B 802

Chain	Residue
B	HIS114
B	CYS149
B	GLN151
B	CYS153
B	HIS157
B	MET160

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO A 563

Chain	Residue
A	HIS233
A	HIS283
A	HIS384
A	HAS801
A	CU1803

---

Functional Information from PROSITE/UniProt

site_id	PS00077
Number of Residues	55
Details	COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWTGHPiVyfwllpayaiiytilpkqaggrlvsdpmarlafllflllstpvgf..HH

Chain	Residue	Details
A	TRP229-HIS283

---

site_id	PS00078
Number of Residues	49
Details	COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHgfhvegtninvevlpgevstvrytfkrpgeyrii......CnqyCglgHqnM

Chain	Residue	Details
B	VAL112-MET160

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	TRANSMEM: Helical

Chain	Residue	Details
C	LYS4-GLY34
A	VAL74-ALA94
A	LEU105-LEU125
A	ALA144-LEU164
A	VAL187-PHE207
A	LEU227-ILE247
A	LEU267-ASP287
A	VAL300-LEU320
A	ALA345-VAL365
A	PHE385-LEU405
A	LEU420-HIS440
A	VAL471-VAL491
A	ILE527-VAL547

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-formylmethionine => ECO:0000269|PubMed:11152118

Chain	Residue	Details
C	MET1
A	HIS386
A	HIS384

---

site_id	SWS_FT_FI3
Number of Residues	129
Details	TOPO_DOM: Periplasmic

Chain	Residue	Details
B	THR39-GLU168
A	TYR237

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
B	HIS114
B	CYS149
B	CYS153
B	HIS157

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr)

Chain	Residue	Details
A	TYR237
A	HIS233

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 735

Chain	Residue	Details
B	PHE86	electron shuttle
B	PHE88	electron shuttle
A	HIS384	electron shuttle
A	PHE385	electron shuttle
A	HIS386	electron shuttle
A	ARG449	electron shuttle
A	ARG450	electron shuttle

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