EC number:1.9.3.1

Enzyme

Download
EC Tree
     1. Oxidoreductases
        1.9 Acting on a heme group of donors
            1.9.3 With oxygen as acceptor
ID:1.9.3.1
Description:Cytochrome-c oxidase.
Alternative Name: Warburg's respiratory enzyme.
Cytochrome oxidase.
Cytochrome aa3.
Cytochrome a3.
Complex IV (mitochondrial electron transport).
Prosite: PDOC00663; PDOC00075; PDOC00074;
PDB:
PDBScop
5WEH 8029226; 8041605; 8029228; 8041607; 8028512; 8028517; 8040891; 8040896; 8028508; 8040887; 8029226; 8041605; 8029228; 8041607; 8028512; 8028517; 8040891; 8040896; 8028508; 8040887;
1M57 8029226; 8041605; 8029228; 8041607; 8028512; 8028517; 8040891; 8040896; 8028508; 8040887; 8029226; 8041605; 8029228; 8041607; 8028512; 8028517; 8040891; 8040896; 8028508; 8040887;
1M56 8029226; 8029228; 8041605; 8041607; 8028512; 8028517; 8040891; 8040896; 8028508; 8040887; 8029226; 8041605; 8028512; 8028517; 8040891; 8040896; 8028508; 8040887; 8029228; 8041607;
3EHB 8028674; 8028675; 8041053; 8041054; 8025424; 8037803;
6CI0 8028512; 8028517; 8040891; 8040896; 8028508; 8040887; 8028512; 8028517; 8040891; 8040896; 8028508; 8040887;
 » show all
Cath: 1.10.287.70; 1.10.287.90; 1.10.760.10; 1.20.1070.10; 1.20.120.80; 1.20.210.10; 1.20.5.160; 3.40.30.10; 2.60.260.40; 2.60.40.2600;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.9.3.1
BRENDA Enzyme Link: BRENDA 1.9.3.1
KEGG Enzyme Link: KEGG1.9.3.1
BioCyc Enzyme Link: BioCyc 1.9.3.1
ExPASy Enzyme Link: ExPASy1.9.3.1
EC2PDB Enzyme Link: EC2PDB 1.9.3.1
ExplorEnz Enzyme Link: ExplorEnz 1.9.3.1
PRIAM enzyme-specific profiles Link: PRIAM 1.9.3.1
IntEnz Enzyme Link: IntEnz 1.9.3.1
MEDLINE Enzyme Link: MEDLINE 1.9.3.1

EC number:1.9.3.1

MSA:

1.9.3.1;
Phylogenetic Tree:

1.9.3.1;
Uniprot:
M-CSA:
RHEA:11436 4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] + 2 H2O
RULE(radius=1) [Fe+2;H0:1].[Fe+2;H0:2].[Fe+2;H0:3].[Fe+2;H0:4].[H+;H0:5].[H+;H0:6].[H+;H0:7].[H+;H0:8].[O;H0;+0:9]=[O;H0;+0:10]>>[Fe+3;H0:1].[Fe+3;H0:2].[Fe+3;H0:3].[Fe+3;H0:4].[OH2;+0:9].[OH2;+0:10]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Studies on cytochrome oxidase. III. Improved preparation and some properties.YONETANI T1961 Jun13787373
Studies on cytochrome oxidase. II. Steady state properties.YONETANI T1960 Nov13787372