2KV1
Insights into Function, Catalytic Mechanism and Fold Evolution of Mouse Selenoprotein Methionine Sulfoxide Reductase B1 through Structural Analysis
Replaces: 2KAOFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003779 | molecular_function | actin binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005856 | cellular_component | cytoskeleton |
A | 0008270 | molecular_function | zinc ion binding |
A | 0015629 | cellular_component | actin cytoskeleton |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0030041 | biological_process | actin filament polymerization |
A | 0030091 | biological_process | protein repair |
A | 0033743 | molecular_function | peptide-methionine (R)-S-oxide reductase activity |
A | 0033745 | molecular_function | L-methionine-(R)-S-oxide reductase activity |
A | 0045087 | biological_process | innate immune response |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 125 |
Chain | Residue |
A | CYS23 |
A | CYS26 |
A | CYS71 |
A | CYS74 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01126 |
Chain | Residue | Details |
A | CYS95 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01126, ECO:0000269|PubMed:20605785, ECO:0000312|PDB:2KV1 |
Chain | Residue | Details |
A | CYS23 | |
A | CYS26 | |
A | CYS71 | |
A | CYS74 |