Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3S8G

1.8 A structure of ba3 cytochrome c oxidase mutant (A120F) from Thermus thermophilus in lipid environment

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	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	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	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM A 800

Chain	Residue
A	GLY39
A	ALA77
A	LEU132
A	TYR133
A	PHE385
A	HIS386
A	ALA390
A	THR394
A	MET432
A	MET435
A	ARG449
A	PRO40
A	ARG450
A	ALA451
A	LEU477
A	HOH579
A	HOH586
A	HOH587
A	GLN42
A	ALA43
A	TYR46
A	TYR65
A	LEU69
A	HIS72
A	ASN76

site_id	AC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE HAS A 801

Chain	Residue
A	TYR133
A	TRP229
A	VAL236
A	TYR237
A	HIS282
A	HIS283
A	SER309
A	LEU310
A	ALA313
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	PER563
A	HOH589
A	HOH609
A	HOH610
A	HOH613

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 803

Chain	Residue
A	HIS233
A	HIS282
A	HIS283
A	PER563

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PER A 563

Chain	Residue
A	HIS233
A	VAL236
A	HIS283
A	HOH618
A	HAS801
A	CU803

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OLC A 564

Chain	Residue
A	PRO358
A	MET433
A	HIS440
A	OLC565
B	OLC170
C	PHE22
C	ALA32

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OLC A 565

Chain	Residue
A	OLC564
A	OLC578

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OLC A 566

Chain	Residue
A	TYR161
A	OLC574
A	OLC575

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OLC A 567

Chain	Residue
A	PHE213
A	LEU215
A	TRP341
A	TRP426
A	OLC569
A	OLC573

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OLC A 568

Chain	Residue
A	PHE304
A	ASP517
B	LYS16
B	LEU37
B	ALA38
B	OLC172

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OLC A 569

Chain	Residue
A	SER212
A	PHE213
A	GLY214
A	OLC567
A	OLC577
A	HOH1041

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OLC A 570

Chain	Residue
A	TRP111
A	OLC573
A	OLC576

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 571

Chain	Residue
A	TYR161
A	LEU164
A	ASP165
A	ARG168
A	OLC572

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 572

Chain	Residue
A	TRP167
A	ARG168
A	GLY528
A	OLC571
A	HOH1157

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OLC A 573

Chain	Residue
A	GLY104
A	LEU108
A	ALA464
A	VAL468
A	OLC567
A	OLC570
A	OLC574

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OLC A 574

Chain	Residue
A	ASN102
A	GLY104
A	LEU105
A	MET112
A	LEU472
A	OLC566
A	OLC573
A	OLC575

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 575

Chain	Residue
A	ALA416
A	OLC566
A	OLC574
A	HOH1023
A	HOH1245

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 576

Chain	Residue
A	LYS19
A	TYR23
A	TRP107
A	TRP111
A	OLC570

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 577

Chain	Residue
A	ARG337
A	TRP341
A	OLC569
A	HOH1230

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 578

Chain	Residue
A	TRP441
A	OLC565
A	HOH1024
A	HOH1025
B	OLC170

site_id	CC2
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	CC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OLC B 169

Chain	Residue
B	PHE21
B	LEU32
B	TYR35
B	OLC171
C	TYR27
C	PHE31
C	OLC35

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OLC B 170

Chain	Residue
A	TRP441
A	OLC564
A	OLC578
B	ARG141
B	GLU144
B	TYR145
C	ARG33

site_id	CC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OLC B 171

Chain	Residue
B	ALA13
B	TYR14
B	GLY17
B	TRP18
B	PHE21
B	TYR35
B	OLC169
C	ILE12
C	LEU17

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OLC B 172

Chain	Residue
A	OLC568
B	ALA42
B	HOH1046

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OLC C 35

Chain	Residue
B	OLC169
C	ALA28
C	HOH1027

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. WWTGHPiVyfwllpayaiiytilpkqaggklvsdpmarlafllflllstpvgf..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	260
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	64
Details	Transmembrane: {"description":"Helical"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	129
Details	Topological domain: {"description":"Periplasmic"}

Chain

Residue

Details

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)