1TKK
The Structure of a Substrate-Liganded Complex of the L-Ala-D/L-Glu Epimerase from Bacillus subtilis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0006518 | biological_process | peptide metabolic process |
| 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 | 0000287 | molecular_function | magnesium ion binding |
| B | 0006518 | biological_process | peptide metabolic process |
| 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 | 0000287 | molecular_function | magnesium ion binding |
| C | 0006518 | biological_process | peptide metabolic process |
| 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 | 0000287 | molecular_function | magnesium ion binding |
| D | 0006518 | biological_process | peptide metabolic process |
| 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 |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0006518 | biological_process | peptide metabolic process |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0016854 | molecular_function | racemase and epimerase activity |
| E | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| E | 0016998 | biological_process | cell wall macromolecule catabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0071555 | biological_process | cell wall organization |
| E | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0006518 | biological_process | peptide metabolic process |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0016854 | molecular_function | racemase and epimerase activity |
| F | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| F | 0016998 | biological_process | cell wall macromolecule catabolic process |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0071555 | biological_process | cell wall organization |
| F | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0006518 | biological_process | peptide metabolic process |
| G | 0016853 | molecular_function | isomerase activity |
| G | 0016854 | molecular_function | racemase and epimerase activity |
| G | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| G | 0016998 | biological_process | cell wall macromolecule catabolic process |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0071555 | biological_process | cell wall organization |
| G | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0006518 | biological_process | peptide metabolic process |
| H | 0016853 | molecular_function | isomerase activity |
| H | 0016854 | molecular_function | racemase and epimerase activity |
| H | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| H | 0016998 | biological_process | cell wall macromolecule catabolic process |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0071555 | biological_process | cell wall organization |
| H | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1601 |
| Chain | Residue |
| A | LYS160 |
| A | ASP191 |
| A | GLU219 |
| A | ASP244 |
| A | GLU2471 |
| A | HOH2472 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1602 |
| Chain | Residue |
| B | ASP244 |
| B | GLU2473 |
| B | HOH2474 |
| B | LYS160 |
| B | ASP191 |
| B | GLU219 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 1603 |
| Chain | Residue |
| C | LYS160 |
| C | ASP191 |
| C | GLU219 |
| C | ASP244 |
| C | GLU2475 |
| C | HOH2476 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 1604 |
| Chain | Residue |
| D | ASP191 |
| D | ASN193 |
| D | GLU219 |
| D | ASP244 |
| D | GLU2477 |
| D | HOH2478 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 1605 |
| Chain | Residue |
| E | ASP191 |
| E | GLU219 |
| E | ASP244 |
| E | GLU2479 |
| E | HOH2480 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 1606 |
| Chain | Residue |
| F | ASP191 |
| F | GLU219 |
| F | ASP244 |
| F | GLU2481 |
| F | HOH2482 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG G 1607 |
| Chain | Residue |
| G | LYS160 |
| G | ASP191 |
| G | GLU219 |
| G | ASP244 |
| G | GLU2483 |
| G | HOH2484 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG H 1608 |
| Chain | Residue |
| H | LYS160 |
| H | ASP191 |
| H | GLU219 |
| H | ASP244 |
| H | GLU2485 |
| H | HOH2486 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ALA A 2470 |
| Chain | Residue |
| A | PHE19 |
| A | THR135 |
| A | LYS160 |
| A | LYS162 |
| A | ASP321 |
| A | ASP323 |
| A | GLU2471 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GLU A 2471 |
| Chain | Residue |
| A | PHE19 |
| A | ARG24 |
| A | ILE54 |
| A | LYS160 |
| A | LYS162 |
| A | ASP191 |
| A | ASP244 |
| A | LYS268 |
| A | SER296 |
| A | MET297 |
| A | ILE298 |
| A | MG1601 |
| A | ALA2470 |
| A | HOH2541 |
| A | HOH2577 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ALA B 2472 |
| Chain | Residue |
| B | PHE19 |
| B | THR135 |
| B | LYS160 |
| B | LYS162 |
| B | ASP321 |
| B | ASP323 |
| B | GLU2473 |
| site_id | BC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GLU B 2473 |
| Chain | Residue |
| B | PHE19 |
| B | ARG24 |
| B | ILE54 |
| B | LYS160 |
| B | LYS162 |
| B | ASP191 |
| B | GLU219 |
| B | ASP244 |
| B | LYS268 |
| B | SER296 |
| B | ILE298 |
| B | MG1602 |
| B | ALA2472 |
| B | HOH2484 |
| B | HOH2510 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ALA C 2474 |
| Chain | Residue |
| C | THR135 |
| C | LYS160 |
| C | LYS162 |
| C | ASP321 |
| C | ASP323 |
| C | GLU2475 |
| site_id | BC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE GLU C 2475 |
| Chain | Residue |
| C | LYS160 |
| C | LYS162 |
| C | ASP191 |
| C | ASP244 |
| C | LYS268 |
| C | SER296 |
| C | MET297 |
| C | ILE298 |
| C | MG1603 |
| C | ALA2474 |
| C | HOH2479 |
| C | PHE19 |
| C | ARG24 |
| C | ILE54 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ALA D 2476 |
| Chain | Residue |
| D | PHE19 |
| D | THR135 |
| D | LYS160 |
| D | LYS162 |
| D | ASP321 |
| D | ASP323 |
| D | GLU2477 |
| site_id | BC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GLU D 2477 |
| Chain | Residue |
| D | PHE19 |
| D | ARG24 |
| D | ILE54 |
| D | LYS160 |
| D | LYS162 |
| D | ASP191 |
| D | ASP244 |
| D | LYS268 |
| D | SER296 |
| D | MET297 |
| D | ILE298 |
| D | MG1604 |
| D | ALA2476 |
| D | HOH2521 |
| D | HOH2530 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ALA E 2478 |
| Chain | Residue |
| E | THR135 |
| E | LYS160 |
| E | LYS162 |
| E | ASP321 |
| E | ASP323 |
| E | GLU2479 |
| site_id | BC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GLU E 2479 |
| Chain | Residue |
| E | PHE19 |
| E | ARG24 |
| E | LYS160 |
| E | LYS162 |
| E | ASP244 |
| E | LYS268 |
| E | SER296 |
| E | ILE298 |
| E | MG1605 |
| E | ALA2478 |
| E | HOH2526 |
| E | HOH2528 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ALA F 2480 |
| Chain | Residue |
| F | PHE19 |
| F | THR135 |
| F | LYS160 |
| F | LYS162 |
| F | ASP321 |
| F | ASP323 |
| F | GLU2481 |
| site_id | CC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GLU F 2481 |
| Chain | Residue |
| F | PHE19 |
| F | ARG24 |
| F | ILE54 |
| F | LYS160 |
| F | LYS162 |
| F | ASP191 |
| F | ASP244 |
| F | LYS268 |
| F | SER296 |
| F | MET297 |
| F | ILE298 |
| F | MG1606 |
| F | ALA2480 |
| F | HOH2531 |
| F | HOH2539 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ALA G 2482 |
| Chain | Residue |
| G | PHE19 |
| G | THR135 |
| G | LYS160 |
| G | LYS162 |
| G | SER296 |
| G | ASP321 |
| G | ASP323 |
| G | GLU2483 |
| site_id | CC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GLU G 2483 |
| Chain | Residue |
| G | PHE19 |
| G | ARG24 |
| G | ILE54 |
| G | LYS160 |
| G | LYS162 |
| G | ASP191 |
| G | ASP244 |
| G | LYS268 |
| G | SER296 |
| G | MET297 |
| G | ILE298 |
| G | MG1607 |
| G | ALA2482 |
| G | HOH2519 |
| G | HOH2520 |
| site_id | CC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ALA H 2484 |
| Chain | Residue |
| H | PHE19 |
| H | THR135 |
| H | LYS160 |
| H | LYS162 |
| H | ASP321 |
| H | ASP323 |
| H | GLU2485 |
| site_id | CC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE GLU H 2485 |
| Chain | Residue |
| H | ARG24 |
| H | ILE54 |
| H | LYS160 |
| H | LYS162 |
| H | ASP191 |
| H | ASP244 |
| H | LYS268 |
| H | SER296 |
| H | MET297 |
| H | ILE298 |
| H | MG1608 |
| H | ALA2484 |
| H | HOH2493 |
| H | HOH2550 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor; specific for (R)-substrate epimerization","evidences":[{"source":"PubMed","id":"15301535","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor; specific for (S)-substrate epimerization","evidences":[{"source":"PubMed","id":"15301535","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 56 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15301535","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11747448","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15301535","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| A | ASP321 | |
| A | LYS160 | |
| A | LYS162 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| B | LYS268 | |
| B | LYS162 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| C | LYS268 | |
| C | LYS162 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| D | LYS268 | |
| D | LYS162 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| E | LYS268 | |
| E | LYS162 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| F | LYS268 | |
| F | LYS162 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| G | LYS268 | |
| G | LYS162 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| H | LYS268 | |
| H | LYS162 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| B | ASP321 | |
| B | LYS160 | |
| B | LYS162 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| C | ASP321 | |
| C | LYS160 | |
| C | LYS162 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| D | ASP321 | |
| D | LYS160 | |
| D | LYS162 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| E | ASP321 | |
| E | LYS160 | |
| E | LYS162 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| F | ASP321 | |
| F | LYS160 | |
| F | LYS162 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| G | ASP321 | |
| G | LYS160 | |
| G | LYS162 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| H | ASP321 | |
| H | LYS160 | |
| H | LYS162 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| A | LYS268 | |
| A | LYS162 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 957 |
| Chain | Residue | Details |
| A | LYS162 | proton acceptor, proton donor |
| A | ASP191 | metal ligand |
| A | GLU219 | metal ligand |
| A | ASP244 | metal ligand |
| A | LYS268 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 957 |
| Chain | Residue | Details |
| B | LYS162 | proton acceptor, proton donor |
| B | ASP191 | metal ligand |
| B | GLU219 | metal ligand |
| B | ASP244 | metal ligand |
| B | LYS268 | proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 957 |
| Chain | Residue | Details |
| C | LYS162 | proton acceptor, proton donor |
| C | ASP191 | metal ligand |
| C | GLU219 | metal ligand |
| C | ASP244 | metal ligand |
| C | LYS268 | proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 957 |
| Chain | Residue | Details |
| D | LYS162 | proton acceptor, proton donor |
| D | ASP191 | metal ligand |
| D | GLU219 | metal ligand |
| D | ASP244 | metal ligand |
| D | LYS268 | proton acceptor, proton donor |
| site_id | MCSA5 |
| Number of Residues | 5 |
| Details | M-CSA 957 |
| Chain | Residue | Details |
| E | LYS162 | proton acceptor, proton donor |
| E | ASP191 | metal ligand |
| E | GLU219 | metal ligand |
| E | ASP244 | metal ligand |
| E | LYS268 | proton acceptor, proton donor |
| site_id | MCSA6 |
| Number of Residues | 5 |
| Details | M-CSA 957 |
| Chain | Residue | Details |
| F | LYS162 | proton acceptor, proton donor |
| F | ASP191 | metal ligand |
| F | GLU219 | metal ligand |
| F | ASP244 | metal ligand |
| F | LYS268 | proton acceptor, proton donor |
| site_id | MCSA7 |
| Number of Residues | 5 |
| Details | M-CSA 957 |
| Chain | Residue | Details |
| G | LYS162 | proton acceptor, proton donor |
| G | ASP191 | metal ligand |
| G | GLU219 | metal ligand |
| G | ASP244 | metal ligand |
| G | LYS268 | proton acceptor, proton donor |
| site_id | MCSA8 |
| Number of Residues | 5 |
| Details | M-CSA 957 |
| Chain | Residue | Details |
| H | LYS162 | proton acceptor, proton donor |
| H | ASP191 | metal ligand |
| H | GLU219 | metal ligand |
| H | ASP244 | metal ligand |
| H | LYS268 | proton acceptor, proton donor |
