1EGO
NMR STRUCTURE OF OXIDIZED ESCHERICHIA COLI GLUTAREDOXIN: COMPARISON WITH REDUCED E. COLI GLUTAREDOXIN AND FUNCTIONALLY RELATED PROTEINS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0010134 | biological_process | sulfate assimilation via adenylyl sulfate reduction |
| A | 0015035 | molecular_function | protein-disulfide reductase activity |
| A | 0015036 | molecular_function | disulfide oxidoreductase activity |
| A | 0015038 | molecular_function | glutathione disulfide oxidoreductase activity |
| A | 0019153 | molecular_function | protein-disulfide reductase (glutathione) activity |
| A | 0019345 | biological_process | cysteine biosynthetic process via S-sulfo-L-cysteine |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PROSITE/UniProt
| site_id | PS00195 |
| Number of Residues | 16 |
| Details | GLUTAREDOXIN_1 Glutaredoxin active site. IFgrsgCPYCvrAkd.L |
| Chain | Residue | Details |
| A | ILE5-LEU20 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 84 |
| Details | Domain: {"description":"Glutaredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00686","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"O-AMP-tyrosine; by YdiU","evidences":[{"source":"PubMed","id":"30270044","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1qfn |
| Chain | Residue | Details |
| A | TYR13 | |
| A | ARG8 | |
| A | GLY10 | |
| A | LYS18 | |
| A | TYR72 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 792 |
| Chain | Residue | Details |
| A | ARG8 | enhance reactivity, modifies pKa |
| A | GLY10 | electrostatic stabiliser, proton acceptor, proton donor |
| A | CYS11 | electrofuge, electrophile, nucleophile |
| A | TYR13 | electrostatic stabiliser |
| A | CYS14 | nucleophile, proton donor |
| A | LYS18 | enhance reactivity |
| A | TYR72 | electrostatic stabiliser |
