7R1R
RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| 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 | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| 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 | 270 |
| Details | Domain: {"description":"ATP-cone","evidences":[{"source":"PROSITE-ProRule","id":"PRU00492","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Cysteine radical intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9309223","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R1R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9309223","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R1R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Site: {"description":"Important for hydrogen atom transfer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Site: {"description":"Important for electron transfer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
| 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 | MCSA3 |
| Number of Residues | |
| Details | M-CSA 918 |
| Chain | Residue | Details |
| site_id | MCSA4 |
| Number of Residues | |
| Details | M-CSA 918 |
| Chain | Residue | Details |
