3DEQ
Crystal structure of dipeptide epimerase from Thermotoga maritima complexed with L-Ala-L-Leu dipeptide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016854 | molecular_function | racemase and epimerase activity |
| A | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
| A | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016854 | molecular_function | racemase and epimerase activity |
| B | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| B | 0016998 | biological_process | cell wall macromolecule catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
| B | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016854 | molecular_function | racemase and epimerase activity |
| C | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| C | 0016998 | biological_process | cell wall macromolecule catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0071555 | biological_process | cell wall organization |
| C | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016854 | molecular_function | racemase and epimerase activity |
| D | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| D | 0016998 | biological_process | cell wall macromolecule catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0071555 | biological_process | cell wall organization |
| D | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | ASP188 |
| A | GLU216 |
| A | ASP241 |
| A | LEU412 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | LYS159 |
| B | ASP188 |
| B | GLU216 |
| B | ASP241 |
| B | LEU412 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 401 |
| Chain | Residue |
| C | ASP188 |
| C | GLU216 |
| C | ASP241 |
| C | LEU412 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 401 |
| Chain | Residue |
| D | ASP188 |
| D | GLU216 |
| D | ASP241 |
| D | LEU412 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; specific for (R)-substrate epimerization => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS161 | |
| B | LYS161 | |
| C | LYS161 | |
| D | LYS161 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; specific for (S)-substrate epimerization => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS265 | |
| B | LYS265 | |
| C | LYS265 | |
| D | LYS265 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | THR134 | |
| B | THR134 | |
| B | LYS159 | |
| B | ASP188 | |
| B | ASN190 | |
| B | GLU216 | |
| B | ASP241 | |
| B | CYS292 | |
| B | ASP317 | |
| B | ASP319 | |
| C | THR134 | |
| A | LYS159 | |
| C | LYS159 | |
| C | ASP188 | |
| C | ASN190 | |
| C | GLU216 | |
| C | ASP241 | |
| C | CYS292 | |
| C | ASP317 | |
| C | ASP319 | |
| D | THR134 | |
| D | LYS159 | |
| A | ASP188 | |
| D | ASP188 | |
| D | ASN190 | |
| D | GLU216 | |
| D | ASP241 | |
| D | CYS292 | |
| D | ASP317 | |
| D | ASP319 | |
| A | ASN190 | |
| A | GLU216 | |
| A | ASP241 | |
| A | CYS292 | |
| A | ASP317 | |
| A | ASP319 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| A | ASP317 | |
| A | LYS161 | |
| A | LYS159 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| B | ASP317 | |
| B | LYS161 | |
| B | LYS159 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| C | ASP317 | |
| C | LYS161 | |
| C | LYS159 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| D | ASP317 | |
| D | LYS161 | |
| D | LYS159 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| A | LYS161 | |
| A | LYS265 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| B | LYS161 | |
| B | LYS265 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| C | LYS161 | |
| C | LYS265 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| D | LYS161 | |
| D | LYS265 |
