EC number:1.17.4.1
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.17 Acting on CH or CH2 groups |
| 1.17.4 With a disulfide as acceptor |
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 |
1XSM;
1W69;
1W68;
1H0O;
1H0N;
1UZR;
7R1R;
6R1R;
5R1R;
4R1R;
3R1R;
2XO5;
2XO4;
2XAZ;
2XAY;
2XAX;
2XAW;
2XAV;
2XAP;
2XAK;
2X0X;
2R1R;
1R1R;
5CNV;
4ERM;
1RLR;
2BQ1;
1PEU;
1PEQ;
1PEO;
1PEM;
2R2F;
1R2F;
3OLJ;
3VPO;
3VPN;
3VPM;
2UW2;
1SMS;
1SMQ;
1JK0;
5CNU;
5CNT;
5CNS;
4ERP;
3UUS;
1XIK;
1RNR;
1RIB;
1R65;
1PM2;
1PJ1;
1PJ0;
1PIZ;
1PIY;
1PIU;
1PIM;
1PFR;
1MXR;
1MRR;
1JQC;
1JPR;
1AV8;
2ALX;
6CGN;
6CGM;
6CGL;
6AUI;
5TUS;
5D1Y;
4X3V;
4M1F;
4DR0;
3TBA;
3TB9;
3S8C;
3S8B;
3S8A;
3S87;
3RSR;
3PAW;
3N3B;
3N3A;
3N39;
3N38;
3N37;
3K8T;
3HNF;
3HNE;
3HND;
3HNC;
3HF1;
2ZLG;
2ZLF;
2WGH;
2VUX;
2EUD;
2CVY;
2CVX;
2CVW;
2CVV;
2CVU;
2CVT;
2CVS;
1ZZD;
1ZYZ;
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References
External Links
| UniProtKB Enzyme Link: | UniProtKB 1.17.4.1 |
| BRENDA Enzyme Link: | BRENDA 1.17.4.1 |
| KEGG Enzyme Link: | KEGG1.17.4.1 |
| BioCyc Enzyme Link: | BioCyc 1.17.4.1 |
| ExPASy Enzyme Link: | ExPASy1.17.4.1 |
| EC2PDB Enzyme Link: | EC2PDB 1.17.4.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.17.4.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.17.4.1 |
| IntEnz Enzyme Link: | IntEnz 1.17.4.1 |
| MEDLINE Enzyme Link: | MEDLINE 1.17.4.1 |
| RHEA:23252 | [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[*:4]-[S;H0;+0:5]-[S;H0;+0:6]-[*:7].[OH2;+0:8]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:8].[*:4]-[SH;+0:5].[*:7]-[SH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. | Qiu W, Zhou B, Darwish D, Shao J, Yen Y | 2006 Feb 10 | 16376858 |
| RHEA:28026 | [thioredoxin]-disulfide + dUDP + H2O = [thioredoxin]-dithiol + UDP |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[*:4]-[S;H0;+0:5]-[S;H0;+0:6]-[*:7].[OH2;+0:8]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:8].[*:4]-[SH;+0:5].[*:7]-[SH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. | Qiu W, Zhou B, Darwish D, Shao J, Yen Y | 2006 Feb 10 | 16376858 |
| RHEA:28030 | [thioredoxin]-disulfide + dGDP + H2O = [thioredoxin]-dithiol + GDP |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[*:4]-[S;H0;+0:5]-[S;H0;+0:6]-[*:7].[OH2;+0:8]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:8].[*:4]-[SH;+0:5].[*:7]-[SH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. | Qiu W, Zhou B, Darwish D, Shao J, Yen Y | 2006 Feb 10 | 16376858 |
| RHEA:28034 | [thioredoxin]-disulfide + dADP + H2O = [thioredoxin]-dithiol + ADP |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[*:4]-[S;H0;+0:5]-[S;H0;+0:6]-[*:7].[OH2;+0:8]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:8].[*:4]-[SH;+0:5].[*:7]-[SH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. | Qiu W, Zhou B, Darwish D, Shao J, Yen Y | 2006 Feb 10 | 16376858 |
| RHEA:28038 | [thioredoxin]-disulfide + dCDP + H2O = [thioredoxin]-dithiol + CDP |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[*:4]-[S;H0;+0:5]-[S;H0;+0:6]-[*:7].[OH2;+0:8]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:8].[*:4]-[SH;+0:5].[*:7]-[SH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. | Qiu W, Zhou B, Darwish D, Shao J, Yen Y | 2006 Feb 10 | 16376858 |