Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QLE

CRYO-STRUCTURE OF THE PARACOCCUS DENITRIFICANS FOUR-SUBUNIT CYTOCHROME C OXIDASE IN THE COMPLETELY OXIDIZED STATE COMPLEXED WITH AN ANTIBODY FV FRAGMENT

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	0009060	biological_process	aerobic respiration
A	0015990	biological_process	electron transport coupled proton transport
A	0016020	cellular_component	membrane
A	0020037	molecular_function	heme binding
A	0022904	biological_process	respiratory electron transport chain
A	0045277	cellular_component	respiratory chain complex IV
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	0016491	molecular_function	oxidoreductase activity
B	0022900	biological_process	electron transport chain
B	0042773	biological_process	ATP synthesis coupled electron transport
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	0009055	molecular_function	electron transfer activity
C	0009060	biological_process	aerobic respiration
C	0016020	cellular_component	membrane
C	0019646	biological_process	aerobic electron transport chain
C	0022904	biological_process	respiratory electron transport chain
C	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU Y 2

Chain	Residue
A	HIS276
A	HIS325
A	HIS326

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA Z 1

Chain	Residue
A	GLU56
A	HIS59
A	PRO60
A	GLY61
A	GLN63

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN Z 2

Chain	Residue
A	ASP404
B	GLU218
A	HIS403

site_id	AC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE HEA X 1

Chain	Residue
A	LEU36
A	ALA39
A	GLY40
A	VAL47
A	THR50
A	ARG54
A	TRP87
A	ILE91
A	HIS94
A	MET98
A	VAL103
A	ALA106
A	GLY163
A	TRP164
A	TYR406
A	VAL409
A	PHE412
A	HIS413
A	MET416
A	SER417
A	VAL421
A	MET452
A	ARG473
A	ARG474
A	TYR475
A	PHE500

site_id	AC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEA X 2

Chain	Residue
A	TRP164
A	VAL279
A	TYR280
A	HIS325
A	HIS326
A	ALA348
A	THR351
A	GLY387
A	GLY390
A	VAL391
A	LEU393
A	SER394
A	ASP399
A	HIS403
A	VAL408
A	HIS411
A	PHE412
A	VAL415
A	ARG473
A	ARG474
B	VAL45
B	ILE88

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CUA Y 1

Chain	Residue
B	HIS181
B	CYS216
B	GLU218
B	CYS220
B	HIS224
B	MET227

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PC1 P 2

Chain	Residue
A	LEU233
A	TRP323
A	GLN336
A	TYR339
B	ARG198
C	VAL102
C	TRP106
C	LYS110
C	TYR114
C	PRO121
C	ASP124
D	SER37
D	ASN48

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PC1 P 3

Chain	Residue
C	LEU55
C	TRP66
C	VAL69
C	VAL70
C	GLY73
C	GLU74
C	HIS78
C	LEU86
C	PHE90
C	ILE222
C	ILE225
C	PHE226
C	VAL229
C	ARG233
C	GLN238
C	THR240
C	GLN243
C	HIS244
C	VAL245
C	GLY246

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. WFFGHPeVyiiilpgfgiishvistfakkpifgylpmvlamaaigilgfvvwa..HH

Chain	Residue	Details
A	TRP272-HIS326

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

Chain	Residue	Details
B	VAL179-MET227

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	31
Details	TRANSMEM: Helical

Chain	Residue	Details
D	ARG17-ASN48
C	HIS78-THR79
C	ASP167-ARG168
C	GLN238-HIS244

site_id	SWS_FT_FI2
Number of Residues	1
Details	TOPO_DOM: Periplasmic

Chain	Residue	Details
D	SER49
C	TRP49-GLU77
C	PRO80-PRO115
C	LEU140-GLY166
C	LYS169-ALA197
C	VAL204-GLY237

site_id	SWS_FT_FI3
Number of Residues	39
Details	TOPO_DOM: Periplasmic

Chain	Residue	Details
C	GLY37-PRO48
C	MET116-HIS139
C	PHE198-THR203

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
B	HIS181
B	CYS216
B	GLU218
B	CYS220
B	HIS224
B	MET227

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269\|PubMed:2820725

Chain	Residue	Details
B	GLN1

site_id	SWS_FT_FI6
Number of Residues	29
Details	TRANSMEM: Helical; Name=IV

Chain	Residue	Details
A	TYR177-ASN206

site_id	SWS_FT_FI7
Number of Residues	33
Details	TRANSMEM: Helical; Name=V

Chain	Residue	Details
A	PRO218-PHE251

site_id	SWS_FT_FI8
Number of Residues	36
Details	TRANSMEM: Helical; Name=VI

Chain	Residue	Details
A	ASP263-LYS299

site_id	SWS_FT_FI9
Number of Residues	27
Details	TRANSMEM: Helical; Name=VII

Chain	Residue	Details
A	GLY304-GLY331

site_id	SWS_FT_FI10
Number of Residues	31
Details	TRANSMEM: Helical; Name=VIII

Chain	Residue	Details
A	SER333-GLY364

site_id	SWS_FT_FI11
Number of Residues	25
Details	TRANSMEM: Helical; Name=IX

Chain	Residue	Details
A	LYS370-GLN395

site_id	SWS_FT_FI12
Number of Residues	32
Details	TRANSMEM: Helical; Name=X

Chain	Residue	Details
A	THR405-GLY437

site_id	SWS_FT_FI13
Number of Residues	28
Details	TRANSMEM: Helical; Name=XI

Chain	Residue	Details
A	PRO441-GLN469

site_id	SWS_FT_FI14
Number of Residues	35
Details	TRANSMEM: Helical; Name=XII

Chain	Residue	Details
A	PRO479-GLY514

site_id	SWS_FT_FI15
Number of Residues	3
Details	BINDING: axial binding residue

Chain	Residue	Details
A	HIS94
A	HIS411
A	HIS413

site_id	SWS_FT_FI16
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	HIS276
A	TYR280
A	HIS325
A	HIS326

site_id	SWS_FT_FI17
Number of Residues	2
Details	CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr)

Chain	Residue	Details
A	HIS276
A	TYR280

Catalytic Information from CSA

site_id	CSA1
Number of Residues	7
Details	Annotated By Reference To The Literature 1ar1

Chain	Residue	Details
A	ARG473
A	TYR280
A	HIS411
A	HIS276
A	ARG474
A	PHE412
A	HIS413

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ar1

Chain	Residue	Details
A	GLU278
A	LYS354

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)