Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4G7Q

Structure of Recombinant Cytochrome ba3 Oxidase mutant V236L 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	5
Details	BINDING SITE FOR RESIDUE CU A 601

Chain	Residue
A	HIS233
A	LEU236
A	HIS282
A	HIS283
A	PER604

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM A 602

Chain	Residue
A	TYR46
A	TYR65
A	LEU69
A	HIS72
A	ASN76
A	ALA77
A	TYR133
A	PHE385
A	HIS386
A	ALA390
A	THR394
A	MET432
A	MET435
A	ARG449
A	ARG450
A	ALA451
A	LEU477
A	HOH703
A	HOH706
A	GLY39
A	PRO40
A	GLN42
A	ALA43

site_id	AC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE HAS A 603

Chain	Residue
A	TYR133
A	TRP229
A	LEU236
A	TYR237
A	TRP239
A	LEU240
A	HIS282
A	HIS283
A	SER309
A	LEU310
A	ALA313
A	LEU320
A	LEU353
A	PHE356
A	GLY360
A	GLY363
A	ASN366
A	ALA367
A	ASP372
A	HIS376
A	HIS384
A	PHE385
A	GLN388
A	ARG449
A	PER604
A	HOH704
A	HOH713

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PER A 604

Chain	Residue
A	HIS233
A	LEU236
A	HIS282
A	HIS283
A	CU601
A	HAS603

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 605

Chain	Residue
A	LEU105
A	TYR161
A	VAL476
A	OLC612

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OLC A 606

Chain	Residue
A	PHE213
A	LEU215
A	TRP341
A	VAL347
A	TRP426
A	LEU430
A	OLC607
A	OLC611
A	OLC612

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OLC A 607

Chain	Residue
A	LYS140
A	TRP143
A	SER212
A	PHE213
A	LEU430
A	OLC606
A	OLC614

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OLC A 608

Chain	Residue
A	TRP111
A	OLC611

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 609

Chain	Residue
A	TYR161
A	LEU164
A	ASP165
A	ARG168

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 610

Chain	Residue
A	TRP167
A	ARG168
A	GLY528
A	HOH717

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OLC A 611

Chain	Residue
A	GLY104
A	ALA464
A	VAL468
A	OLC606
A	OLC608
A	OLC612

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OLC A 612

Chain	Residue
A	LEU108
A	LEU472
A	OLC605
A	OLC606
A	OLC611
A	OLC613
A	ASN102
A	GLY104

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 613

Chain	Residue
A	VAL216
A	ALA416
A	ARG419
A	OLC612
A	HOH752

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 614

Chain	Residue
A	ARG337
A	TRP341
A	LEU430
A	OLC607

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CUA B 201

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

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC B 202

Chain	Residue
B	PHE21
B	TYR35
B	OLC204
C	PHE31

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OLC B 203

Chain	Residue
A	TRP441
B	ARG141
B	GLU144
B	TYR145
C	ARG33
C	OLC101

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OLC B 204

Chain	Residue
B	ALA13
B	TYR14
B	GLY17
B	TYR35
B	OLC202
C	ILE12

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OLC B 205

Chain	Residue
A	THR293
B	ALA42

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OLC C 101

Chain	Residue
A	PRO358
A	HIS440
B	OLC203
C	PHE22
C	GLY25
C	ALA28
C	VAL29
C	OLC102

site_id	CC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OLC C 102

Chain	Residue
C	THR18
C	PHE22
C	OLC101

Functional Information from PROSITE/UniProt

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

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

Chain	Residue	Details
C	MET1
A	HIS384
A	HIS386

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	HIS233
A	TYR237

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)