1MBB
OXIDOREDUCTASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008762 | molecular_function | UDP-N-acetylmuramate dehydrogenase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
| A | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE EEB A 402 |
| Chain | Residue |
| A | ALA124 |
| A | PHE231 |
| A | ASN233 |
| A | PRO252 |
| A | TYR254 |
| A | ALA264 |
| A | GLY266 |
| A | TRP267 |
| A | ASP270 |
| A | LYS275 |
| A | GLN288 |
| A | TYR125 |
| A | ALA289 |
| A | GLU325 |
| A | FAD401 |
| A | HOH514 |
| A | HOH520 |
| A | HOH521 |
| A | HOH526 |
| A | HOH530 |
| A | HOH604 |
| A | HOH605 |
| A | TYR158 |
| A | ARG159 |
| A | TYR190 |
| A | LYS217 |
| A | LEU218 |
| A | GLY228 |
| A | SER229 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD A 401 |
| Chain | Residue |
| A | LEU44 |
| A | ILE45 |
| A | LEU46 |
| A | GLY47 |
| A | GLU48 |
| A | GLY49 |
| A | SER50 |
| A | ASN51 |
| A | VAL52 |
| A | ASN65 |
| A | ILE110 |
| A | PRO111 |
| A | GLY112 |
| A | CYS113 |
| A | SER116 |
| A | ILE119 |
| A | GLN120 |
| A | ILE122 |
| A | GLY123 |
| A | ALA124 |
| A | ARG159 |
| A | ALA172 |
| A | ILE173 |
| A | ARG214 |
| A | ASN226 |
| A | GLY228 |
| A | ARG327 |
| A | EEB402 |
| A | HOH564 |
| A | HOH566 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 170 |
| Details | Domain: {"description":"FAD-binding PCMH-type"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 8634262, 9020777 |
| Chain | Residue | Details |
| A | SER229 | |
| A | GLU325 | |
| A | ARG159 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 353 |
| Chain | Residue | Details |
| A | ARG159 | attractive charge-charge interaction, electrostatic stabiliser, increase electrophilicity |
| A | SER229 | activator, proton acceptor, proton donor |
| A | GLU325 | activator, attractive charge-charge interaction, electrostatic stabiliser, increase basicity, increase electrophilicity, proton acceptor, proton donor |
