7VDY
Crystal structure of O-ureidoserine racemase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0008837 | molecular_function | diaminopimelate epimerase activity |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0016853 | molecular_function | isomerase activity |
A | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
A | 0017000 | biological_process | antibiotic biosynthetic process |
B | 0005737 | cellular_component | cytoplasm |
B | 0008837 | molecular_function | diaminopimelate epimerase activity |
B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
B | 0016853 | molecular_function | isomerase activity |
B | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
B | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P44859 |
Chain | Residue | Details |
A | CYS81 | |
B | CYS81 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P44859 |
Chain | Residue | Details |
A | CYS227 | |
B | CYS227 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P44859 |
Chain | Residue | Details |
A | ASN20 | |
B | ASN200 | |
B | GLU218 | |
B | GLY228 | |
A | GLY82 | |
A | ASN167 | |
A | ASN200 | |
A | GLU218 | |
A | GLY228 | |
B | ASN20 | |
B | GLY82 | |
B | ASN167 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000250|UniProtKB:P44859 |
Chain | Residue | Details |
A | HIS169 | |
A | GLU218 | |
B | HIS169 | |
B | GLU218 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Important for dimerization => ECO:0000250|UniProtKB:P0A6K1 |
Chain | Residue | Details |
A | TYR278 | |
B | TYR278 |