4IJZ
Crystal structure of diaminopimelate epimerase from Escherichia coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008047 | molecular_function | enzyme activator activity |
A | 0008837 | molecular_function | diaminopimelate epimerase activity |
A | 0009085 | biological_process | lysine biosynthetic process |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0016853 | molecular_function | isomerase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008047 | molecular_function | enzyme activator activity |
B | 0008837 | molecular_function | diaminopimelate epimerase activity |
B | 0009085 | biological_process | lysine biosynthetic process |
B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
B | 0016853 | molecular_function | isomerase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE NO3 A 301 |
Chain | Residue |
A | ALA132 |
A | ASN133 |
A | LYS134 |
A | TYR139 |
A | ARG184 |
A | HOH516 |
B | PHE24 |
B | PHE25 |
B | SER26 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO3 A 302 |
Chain | Residue |
A | VAL23 |
A | GLU49 |
A | HOH437 |
B | ARG142 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE NO3 B 301 |
Chain | Residue |
A | PHE24 |
A | PHE25 |
A | SER26 |
B | ALA132 |
B | ASN133 |
B | LYS134 |
B | TYR139 |
B | ARG184 |
B | HOH427 |
B | HOH551 |
Functional Information from PROSITE/UniProt
site_id | PS01326 |
Number of Residues | 15 |
Details | DAP_EPIMERASE Diaminopimelate epimerase signature. NaDGSevaqCGNGaR |
Chain | Residue | Details |
A | ASN64-ARG78 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00197 |
Chain | Residue | Details |
A | CYS73 | |
B | CYS73 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00197 |
Chain | Residue | Details |
A | CYS217 | |
B | CYS217 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00197 |
Chain | Residue | Details |
B | ASN64 | |
B | GLY74 | |
B | ASN157 | |
B | ASN190 | |
B | GLU208 | |
B | GLY218 | |
A | GLY74 | |
A | ASN157 | |
A | ASN190 | |
A | GLU208 | |
A | GLY218 | |
B | ASN11 | |
B | GLN44 | |
A | ASN11 | |
A | GLN44 | |
A | ASN64 |
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:0000255|HAMAP-Rule:MF_00197 |
Chain | Residue | Details |
A | HIS159 | |
A | GLU208 | |
B | HIS159 | |
B | GLU208 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Important for dimerization => ECO:0000269|PubMed:23426375 |
Chain | Residue | Details |
A | TYR268 | |
B | TYR268 |