2X7J
Structure of the menaquinone biosynthesis protein MenD from Bacillus subtilis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0009234 | biological_process | menaquinone biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0030145 | molecular_function | manganese ion binding |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0070204 | molecular_function | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0009234 | biological_process | menaquinone biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0030145 | molecular_function | manganese ion binding |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0070204 | molecular_function | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0009234 | biological_process | menaquinone biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0030145 | molecular_function | manganese ion binding |
C | 0030976 | molecular_function | thiamine pyrophosphate binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0070204 | molecular_function | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0009234 | biological_process | menaquinone biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0030145 | molecular_function | manganese ion binding |
D | 0030976 | molecular_function | thiamine pyrophosphate binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0070204 | molecular_function | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE TPP A 601 |
Chain | Residue |
A | SER405 |
A | ASN484 |
A | GLY486 |
A | GLY487 |
A | GLY488 |
A | ILE489 |
A | PHE490 |
A | MN602 |
A | HOH2200 |
A | HOH2213 |
A | HOH2237 |
A | MET406 |
A | HOH2282 |
B | GLU54 |
B | GLN117 |
B | EDO603 |
A | ASN431 |
A | ILE433 |
A | ASP434 |
A | GLY456 |
A | ASP457 |
A | LEU458 |
A | SER459 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 602 |
Chain | Residue |
A | ASP457 |
A | ASN484 |
A | GLY486 |
A | TPP601 |
A | HOH2237 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 603 |
Chain | Residue |
A | GLY30 |
A | SER31 |
A | ARG32 |
A | THR77 |
A | ARG106 |
A | GLN117 |
B | PHE490 |
B | TPP601 |
site_id | AC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE TPP B 601 |
Chain | Residue |
A | GLU54 |
A | GLN117 |
A | EDO603 |
B | SER405 |
B | MET406 |
B | ASN431 |
B | ILE433 |
B | ASP434 |
B | GLY456 |
B | ASP457 |
B | LEU458 |
B | SER459 |
B | ASN484 |
B | GLY486 |
B | GLY487 |
B | GLY488 |
B | ILE489 |
B | MN602 |
B | HOH2155 |
B | HOH2238 |
B | HOH2239 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 602 |
Chain | Residue |
B | ASP457 |
B | ASN484 |
B | GLY486 |
B | TPP601 |
B | HOH2239 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 603 |
Chain | Residue |
A | PHE490 |
A | TPP601 |
B | GLY30 |
B | SER31 |
B | ARG32 |
B | THR77 |
B | GLN117 |
site_id | AC7 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE TPP C 601 |
Chain | Residue |
C | SER405 |
C | MET406 |
C | PRO407 |
C | ASN431 |
C | GLY432 |
C | ILE433 |
C | ASP434 |
C | GLY456 |
C | ASP457 |
C | LEU458 |
C | SER459 |
C | ASN484 |
C | GLY486 |
C | GLY487 |
C | GLY488 |
C | ILE489 |
C | PHE490 |
C | MN602 |
C | HOH2251 |
C | HOH2252 |
C | HOH2253 |
D | PRO29 |
D | GLU54 |
D | THR80 |
D | GLN117 |
D | EDO603 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN C 602 |
Chain | Residue |
C | HOH2253 |
C | ASP457 |
C | ASN484 |
C | GLY486 |
C | TPP601 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 603 |
Chain | Residue |
C | GLY30 |
C | SER31 |
C | ARG32 |
C | THR77 |
C | GLN117 |
D | PHE490 |
D | TPP601 |
site_id | BC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE TPP D 601 |
Chain | Residue |
C | PRO29 |
C | GLU54 |
C | THR80 |
C | GLN117 |
C | EDO603 |
D | SER405 |
D | MET406 |
D | ASN431 |
D | ILE433 |
D | ASP434 |
D | GLY456 |
D | ASP457 |
D | LEU458 |
D | SER459 |
D | ASN484 |
D | GLY486 |
D | GLY487 |
D | GLY488 |
D | ILE489 |
D | PHE490 |
D | MN602 |
D | HOH2206 |
D | HOH2290 |
D | HOH2291 |
D | HOH2292 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN D 602 |
Chain | Residue |
D | ASP457 |
D | ASN484 |
D | GLY486 |
D | TPP601 |
D | HOH2292 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO D 603 |
Chain | Residue |
C | PHE490 |
C | TPP601 |
D | GLY30 |
D | SER31 |
D | ARG32 |
D | THR77 |
D | GLN117 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA D 1581 |
Chain | Residue |
D | CYS40 |
D | ALA41 |
D | HIS43 |
D | ILE46 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 1581 |
Chain | Residue |
A | CYS40 |
A | ALA41 |
A | HIS43 |
A | ILE46 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 1581 |
Chain | Residue |
B | CYS40 |
B | ALA41 |
B | HIS43 |
B | ILE46 |
B | HOH2022 |
B | HOH2024 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA C 1579 |
Chain | Residue |
C | CYS40 |
C | ALA41 |
C | HIS43 |
C | ILE46 |
C | HOH2015 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 1582 |
Chain | Residue |
A | ARG32 |
A | PRO107 |
A | LEU110 |
A | LEU173 |
A | ARG174 |
A | GLU175 |
A | HOH2283 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 1582 |
Chain | Residue |
B | ARG32 |
B | PRO107 |
B | LEU110 |
B | LEU173 |
B | ARG174 |
B | GLU175 |
site_id | CC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 D 1582 |
Chain | Residue |
D | ARG32 |
D | PRO107 |
D | LEU110 |
D | ARG174 |
D | GLU175 |
D | HOH2041 |
D | HOH2293 |
site_id | CC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 C 1580 |
Chain | Residue |
C | ARG32 |
C | PRO107 |
C | GLU109 |
C | LEU110 |
C | LEU173 |
C | ARG174 |
C | GLU175 |
C | HOH2254 |
C | HOH2255 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1583 |
Chain | Residue |
A | LYS276 |
A | ARG564 |
A | HOH2284 |
A | HOH2285 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 1583 |
Chain | Residue |
B | LYS276 |
B | ARG564 |
B | HOH2121 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 1581 |
Chain | Residue |
C | LYS276 |
C | PHE492 |
C | ARG564 |
C | HOH2256 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 1583 |
Chain | Residue |
D | LYS276 |
D | PHE492 |
D | ARG564 |
Functional Information from PROSITE/UniProt
site_id | PS00041 |
Number of Residues | 42 |
Details | HTH_ARAC_FAMILY_1 Bacterial regulatory proteins, araC family signature. RVpiIVltAdrphe....LrEVGAPqAInqhflFgnfVKFftDsAL |
Chain | Residue | Details |
A | ARG96-LEU137 |