7R1R
RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| A | 0006457 | biological_process | protein folding |
| A | 0009185 | biological_process | ribonucleoside diphosphate metabolic process |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| A | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044183 | molecular_function | protein folding chaperone |
| B | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| B | 0006457 | biological_process | protein folding |
| B | 0009185 | biological_process | ribonucleoside diphosphate metabolic process |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| B | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0044183 | molecular_function | protein folding chaperone |
| C | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| C | 0006457 | biological_process | protein folding |
| C | 0009185 | biological_process | ribonucleoside diphosphate metabolic process |
| C | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| C | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| C | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0044183 | molecular_function | protein folding chaperone |
Functional Information from PDB Data
| site_id | ACA |
| Number of Residues | 5 |
| Details | ACTIVE SITE WITH GLUTAMATE 441 MUTATED TO GLUTAMINE. |
| Chain | Residue |
| A | CYS225 |
| A | CYS462 |
| A | CYS439 |
| A | ASN437 |
| A | GLN441 |
| site_id | ACB |
| Number of Residues | 5 |
| Details | ACTIVE SITE WITH GLUTAMATE 441 MUTATED TO GLUTAMINE. |
| Chain | Residue |
| B | GLN441 |
| B | CYS225 |
| B | CYS462 |
| B | CYS439 |
| B | ASN437 |
| site_id | ACC |
| Number of Residues | 5 |
| Details | ACTIVE SITE WITH GLUTAMATE 441 MUTATED TO GLUTAMINE. |
| Chain | Residue |
| C | CYS225 |
| C | CYS462 |
| C | CYS439 |
| C | ASN437 |
| C | GLN441 |
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 | GLN441 | |
| B | ASN437 | |
| B | GLN441 | |
| C | ASN437 | |
| C | GLN441 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | ACT_SITE: Cysteine radical intermediate |
| Chain | Residue | Details |
| A | CYS439 | |
| B | CYS439 | |
| C | CYS439 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9309223, ECO:0007744|PDB:3R1R |
| 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 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 21 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9309223, ECO:0007744|PDB:4R1R |
| Chain | Residue | Details |
| A | THR209 | |
| B | ARG262 | |
| B | ARG269 | |
| B | ASN437 | |
| B | GLN441 | |
| B | GLU623 | |
| C | THR209 | |
| C | ASP232 | |
| C | ARG262 | |
| C | ARG269 | |
| C | ASN437 | |
| A | ASP232 | |
| C | GLN441 | |
| C | GLU623 | |
| A | ARG262 | |
| A | ARG269 | |
| A | ASN437 | |
| A | GLN441 | |
| 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 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| 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 | GLN441 | |
| 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 | GLN441 | |
| 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 | GLN441 | |
| 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 | GLN441 | 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 | GLN441 | 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 | GLN441 | 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 |
| Chain | Residue | Details |
