Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
A | 0005524 | molecular_function | ATP binding |
A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
B | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
B | 0005524 | molecular_function | ATP binding |
B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
C | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
C | 0005524 | molecular_function | ATP binding |
C | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
Functional Information from PDB Data
site_id | ACA |
Number of Residues | 5 |
Details | ACTIVE SITE WITH GLUTAMATE 441 MUTATED TO ASPARTATE. |
Chain | Residue |
A | CYS225 |
A | CYS462 |
A | CYS439 |
A | ASN437 |
A | ASP441 |
site_id | ACB |
Number of Residues | 5 |
Details | ACTIVE SITE WITH GLUTAMATE 441 MUTATED TO ASPARTATE. |
Chain | Residue |
B | ASP441 |
B | CYS225 |
B | CYS462 |
B | CYS439 |
B | ASN437 |
site_id | ACC |
Number of Residues | 5 |
Details | ACTIVE SITE WITH GLUTAMATE 441 MUTATED TO ASPARTATE. |
Chain | Residue |
C | CYS225 |
C | CYS462 |
C | CYS439 |
C | ASN437 |
C | ASP441 |
Functional Information from PROSITE/UniProt
site_id | PS00089 |
Number of Residues | 23 |
Details | RIBORED_LARGE Ribonucleotide reductase large subunit signature. WeaLresikthGLRNstlSAlmP |
Chain | Residue | Details |
A | TRP599-PRO621 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | ASN437 | |
A | ASP441 | |
B | ASN437 | |
B | ASP441 | |
C | ASN437 | |
C | ASP441 | |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | ACT_SITE: Cysteine radical intermediate |
Chain | Residue | Details |
A | CYS439 | |
B | CYS439 | |
C | CYS439 | |
Chain | Residue | Details |
A | LYS9 | |
C | GLU15 | |
C | THR55 | |
C | LYS91 | |
A | GLU15 | |
A | THR55 | |
A | LYS91 | |
B | LYS9 | |
B | GLU15 | |
B | THR55 | |
B | LYS91 | |
C | LYS9 | |
Chain | Residue | Details |
A | THR209 | |
B | ARG262 | |
B | ARG269 | |
B | ASN437 | |
B | ASP441 | |
B | GLU623 | |
C | THR209 | |
C | ASP232 | |
C | ARG262 | |
C | ARG269 | |
C | ASN437 | |
A | ASP232 | |
C | ASP441 | |
C | GLU623 | |
A | ARG262 | |
A | ARG269 | |
A | ASN437 | |
A | ASP441 | |
A | GLU623 | |
B | THR209 | |
B | ASP232 | |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | SITE: Important for hydrogen atom transfer |
Chain | Residue | Details |
A | CYS225 | |
A | CYS462 | |
B | CYS225 | |
B | CYS462 | |
C | CYS225 | |
C | CYS462 | |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | SITE: Important for electron transfer |
Chain | Residue | Details |
A | TYR730 | |
A | TYR731 | |
B | TYR730 | |
B | TYR731 | |
C | TYR730 | |
C | TYR731 | |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | SITE: Interacts with thioredoxin/glutaredoxin |
Chain | Residue | Details |
A | CYS754 | |
A | CYS759 | |
B | CYS754 | |
B | CYS759 | |
C | CYS754 | |
C | CYS759 | |
Chain | Residue | Details |
A | LYS283 | |
B | LYS283 | |
C | LYS283 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 3r1r |
Chain | Residue | Details |
A | ASP441 | |
A | CYS462 | |
A | CYS439 | |
A | CYS225 | |
A | ASN437 | |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 3r1r |
Chain | Residue | Details |
B | ASP441 | |
B | CYS462 | |
B | CYS439 | |
B | CYS225 | |
B | ASN437 | |
site_id | CSA3 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 3r1r |
Chain | Residue | Details |
C | ASP441 | |
C | CYS462 | |
C | CYS439 | |
C | CYS225 | |
C | ASN437 | |
site_id | MCSA1 |
Number of Residues | |
Details | M-CSA 918 |
Chain | Residue | Details |
A | CYS225 | proton donor |
A | ASN437 | |
A | CYS439 | hydrogen radical acceptor, hydrogen radical donor, single electron acceptor |
A | ASP441 | proton acceptor |
A | CYS462 | |
A | TYR730 | pi-pi interaction, single electron relay |
A | TYR731 | pi-pi interaction, single electron relay |
site_id | MCSA2 |
Number of Residues | |
Details | M-CSA 918 |
Chain | Residue | Details |
B | CYS225 | proton donor |
B | ASN437 | |
B | CYS439 | hydrogen radical acceptor, hydrogen radical donor, single electron acceptor |
B | ASP441 | proton acceptor |
B | CYS462 | |
B | TYR730 | pi-pi interaction, single electron relay |
B | TYR731 | pi-pi interaction, single electron relay |
site_id | MCSA3 |
Number of Residues | |
Details | M-CSA 918 |
Chain | Residue | Details |
C | CYS225 | proton donor |
C | ASN437 | |
C | CYS439 | hydrogen radical acceptor, hydrogen radical donor, single electron acceptor |
C | ASP441 | proton acceptor |
C | CYS462 | |
C | TYR730 | pi-pi interaction, single electron relay |
C | TYR731 | pi-pi interaction, single electron relay |
site_id | MCSA4 |
Number of Residues | |
Details | M-CSA 918 |