Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0009234 | biological_process | menaquinone biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0009234 | biological_process | menaquinone biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0009234 | biological_process | menaquinone biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0009234 | biological_process | menaquinone biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 1377 |
Chain | Residue |
A | LYS168 |
A | ASP195 |
A | GLU220 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 2377 |
Chain | Residue |
B | LYS168 |
B | ASP195 |
B | GLU220 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 3377 |
Chain | Residue |
C | ASP245 |
C | NLQ1376 |
C | LYS168 |
C | ASP195 |
C | GLU220 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 4377 |
Chain | Residue |
D | ASP195 |
D | ASN197 |
D | GLU220 |
D | GLN221 |
D | ASP245 |
D | GLU246 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE NLQ C 1376 |
Chain | Residue |
C | PHE26 |
C | SER142 |
C | LYS170 |
C | LYS269 |
C | GLY297 |
C | MET298 |
C | LEU299 |
C | TYR329 |
C | MG3377 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE NLQ D 2376 |
Chain | Residue |
D | PHE26 |
D | GLN33 |
D | TYR62 |
D | LYS170 |
D | LYS269 |
D | GLY297 |
D | MET298 |
D | LEU299 |
D | TYR329 |
D | HOH4525 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS170 | |
B | LYS170 | |
C | LYS170 | |
D | LYS170 | |
Chain | Residue | Details |
A | LYS269 | |
B | LYS269 | |
C | LYS269 | |
D | LYS269 | |
Chain | Residue | Details |
A | SER142 | |
C | LYS168 | |
C | LYS269 | |
C | LEU299 | |
D | SER142 | |
D | LYS168 | |
D | LYS269 | |
D | LEU299 | |
A | LYS168 | |
A | LYS269 | |
A | LEU299 | |
B | SER142 | |
B | LYS168 | |
B | LYS269 | |
B | LEU299 | |
C | SER142 | |
Chain | Residue | Details |
A | ASP195 | |
A | GLU220 | |
B | ASP195 | |
B | GLU220 | |
C | ASP195 | |
C | GLU220 | |
D | ASP195 | |
D | GLU220 | |
Chain | Residue | Details |
A | ASP245 | |
B | ASP245 | |
C | ASP245 | |
D | ASP245 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r6w |
Chain | Residue | Details |
A | LYS269 | |
A | LYS168 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r6w |
Chain | Residue | Details |
B | LYS269 | |
B | LYS168 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r6w |
Chain | Residue | Details |
C | LYS269 | |
C | LYS168 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r6w |
Chain | Residue | Details |
D | LYS269 | |
D | LYS168 | |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r6w |
Chain | Residue | Details |
A | LYS170 | |
A | LYS269 | |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r6w |
Chain | Residue | Details |
B | LYS170 | |
B | LYS269 | |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r6w |
Chain | Residue | Details |
C | LYS170 | |
C | LYS269 | |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r6w |
Chain | Residue | Details |
D | LYS170 | |
D | LYS269 | |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 377 |
Chain | Residue | Details |
A | SER142 | transition state stabiliser |
A | LYS168 | transition state stabiliser |
A | LYS170 | proton donor |
A | ASP195 | metal ligand |
A | GLU220 | metal ligand |
A | ASP245 | metal ligand |
A | LYS269 | proton acceptor |
A | GLY297 | transition state stabiliser |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 377 |
Chain | Residue | Details |
B | SER142 | transition state stabiliser |
B | LYS168 | transition state stabiliser |
B | LYS170 | proton donor |
B | ASP195 | metal ligand |
B | GLU220 | metal ligand |
B | ASP245 | metal ligand |
B | LYS269 | proton acceptor |
B | GLY297 | transition state stabiliser |
site_id | MCSA3 |
Number of Residues | 8 |
Details | M-CSA 377 |
Chain | Residue | Details |
C | SER142 | transition state stabiliser |
C | LYS168 | transition state stabiliser |
C | LYS170 | proton donor |
C | ASP195 | metal ligand |
C | GLU220 | metal ligand |
C | ASP245 | metal ligand |
C | LYS269 | proton acceptor |
C | GLY297 | transition state stabiliser |
site_id | MCSA4 |
Number of Residues | 8 |
Details | M-CSA 377 |
Chain | Residue | Details |
D | SER142 | transition state stabiliser |
D | LYS168 | transition state stabiliser |
D | LYS170 | proton donor |
D | ASP195 | metal ligand |
D | GLU220 | metal ligand |
D | ASP245 | metal ligand |
D | LYS269 | proton acceptor |
D | GLY297 | transition state stabiliser |