5NDC

Structure of ba3-type cytochrome c oxidase from Thermus thermophilus by serial femtosecond crystallography

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	0016020	cellular_component	membrane
C	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue CU A 601

Chain	Residue
A	HIS233
A	HIS282
A	HIS283
A	HOH752

---

site_id	AC2
Number of Residues	20
Details	binding site for residue HEM A 602

Chain	Residue
A	HIS72
A	ASN76
A	LEU132
A	TYR133
A	PHE385
A	HIS386
A	VAL389
A	ALA390
A	THR394
A	MET432
A	ARG449
A	ARG450
A	ALA451
A	HOH711
A	HOH712
A	GLY39
A	GLN42
A	ALA43
A	TYR46
A	TYR65

---

site_id	AC3
Number of Residues	24
Details	binding site for residue HAS A 603

Chain	Residue
A	TYR133
A	TRP229
A	VAL236
A	TYR237
A	HIS282
A	THR302
A	LEU310
A	ALA313
A	LEU353
A	GLY360
A	GLY363
A	ASN366
A	ALA367
A	ASP372
A	HIS376
A	HIS384
A	PHE385
A	GLN388
A	ARG449
A	HOH707
A	HOH709
A	HOH738
A	HOH743
A	HOH752

---

site_id	AC4
Number of Residues	5
Details	binding site for residue OLC A 604

Chain	Residue
A	PHE213
A	LEU215
A	TRP341
A	TRP426
A	OLC605

---

site_id	AC5
Number of Residues	3
Details	binding site for residue OLC A 605

Chain	Residue
A	TRP143
A	SER212
A	OLC604

---

site_id	AC6
Number of Residues	2
Details	binding site for residue OLC A 606

Chain	Residue
A	TRP111
A	OLC608

---

site_id	AC7
Number of Residues	3
Details	binding site for residue OLC A 607

Chain	Residue
A	TRP167
A	ARG168
A	PHE531

---

site_id	AC8
Number of Residues	3
Details	binding site for residue OLC A 608

Chain	Residue
A	TRP111
A	OLC606
A	OLC609

---

site_id	AC9
Number of Residues	3
Details	binding site for residue OLC A 609

Chain	Residue
A	ASN102
A	LEU472
A	OLC608

---

site_id	AD1
Number of Residues	2
Details	binding site for residue OLC A 610

Chain	Residue
A	ARG419
A	LEU420

---

site_id	AD2
Number of Residues	1
Details	binding site for residue OLC A 611

Chain	Residue
A	TRP341

---

site_id	AD3
Number of Residues	1
Details	binding site for residue OLC A 612

Chain	Residue
B	LEU37

---

site_id	AD4
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	AD5
Number of Residues	5
Details	binding site for residue OLC B 202

Chain	Residue
B	PHE21
B	VAL28
B	LEU32
B	TYR35
C	PHE31

---

site_id	AD6
Number of Residues	2
Details	binding site for residue OLC C 101

Chain	Residue
C	ALA32
C	OLC102

---

site_id	AD7
Number of Residues	4
Details	binding site for residue OLC C 102

Chain	Residue
A	TRP441
A	LEU444
C	ARG33
C	OLC101

---

site_id	AD8
Number of Residues	4
Details	binding site for residue OLC C 103

Chain	Residue
B	TYR14
B	PHE21
B	TYR35
C	ILE12

---

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

---