5JZX
Crystal Structure of UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) from Mycobacterium tuberculosis
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 |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008762 | molecular_function | UDP-N-acetylmuramate dehydrogenase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
| B | 0071949 | molecular_function | FAD binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0008762 | molecular_function | UDP-N-acetylmuramate dehydrogenase activity |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0051301 | biological_process | cell division |
| C | 0071555 | biological_process | cell wall organization |
| C | 0071949 | molecular_function | FAD binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008360 | biological_process | regulation of cell shape |
| D | 0008762 | molecular_function | UDP-N-acetylmuramate dehydrogenase activity |
| D | 0009252 | biological_process | peptidoglycan biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0051301 | biological_process | cell division |
| D | 0071555 | biological_process | cell wall organization |
| D | 0071949 | molecular_function | FAD binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0008360 | biological_process | regulation of cell shape |
| E | 0008762 | molecular_function | UDP-N-acetylmuramate dehydrogenase activity |
| E | 0009252 | biological_process | peptidoglycan biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0051301 | biological_process | cell division |
| E | 0071555 | biological_process | cell wall organization |
| E | 0071949 | molecular_function | FAD binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0008360 | biological_process | regulation of cell shape |
| F | 0008762 | molecular_function | UDP-N-acetylmuramate dehydrogenase activity |
| F | 0009252 | biological_process | peptidoglycan biosynthetic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0051301 | biological_process | cell division |
| F | 0071555 | biological_process | cell wall organization |
| F | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | binding site for residue FAD A 401 |
| Chain | Residue |
| A | THR26 |
| A | ILE127 |
| A | PRO128 |
| A | GLY129 |
| A | SER130 |
| A | ALA133 |
| A | VAL136 |
| A | VAL139 |
| A | GLY140 |
| A | ALA141 |
| A | ARG176 |
| A | VAL65 |
| A | GLY185 |
| A | VAL188 |
| A | VAL191 |
| A | VAL192 |
| A | ARG238 |
| A | SER254 |
| A | VAL255 |
| A | GLY256 |
| A | K402 |
| A | HOH527 |
| A | ALA67 |
| A | HOH548 |
| A | HOH549 |
| A | HOH555 |
| A | HOH592 |
| A | HOH593 |
| A | GLY68 |
| A | GLY69 |
| A | SER70 |
| A | ASN71 |
| A | LEU72 |
| A | LEU86 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue K A 402 |
| Chain | Residue |
| A | ASN71 |
| A | VAL255 |
| A | SER257 |
| A | GLU361 |
| A | FAD401 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue FAD B 401 |
| Chain | Residue |
| B | THR26 |
| B | PHE66 |
| B | ALA67 |
| B | GLY68 |
| B | GLY69 |
| B | SER70 |
| B | ASN71 |
| B | LEU86 |
| B | ILE127 |
| B | PRO128 |
| B | GLY129 |
| B | SER130 |
| B | ALA133 |
| B | VAL136 |
| B | VAL139 |
| B | GLY140 |
| B | ALA141 |
| B | THR190 |
| B | VAL191 |
| B | VAL192 |
| B | ARG238 |
| B | SER254 |
| B | VAL255 |
| B | GLY256 |
| B | VAL363 |
| B | K402 |
| B | HOH510 |
| B | HOH516 |
| B | HOH522 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue K B 402 |
| Chain | Residue |
| B | GLN137 |
| B | FAD401 |
| site_id | AC5 |
| Number of Residues | 34 |
| Details | binding site for residue FAD C 401 |
| Chain | Residue |
| C | HOH501 |
| C | HOH511 |
| C | HOH544 |
| C | HOH560 |
| C | HOH562 |
| C | THR26 |
| C | VAL65 |
| C | PHE66 |
| C | ALA67 |
| C | GLY68 |
| C | GLY69 |
| C | SER70 |
| C | ASN71 |
| C | LEU86 |
| C | ILE127 |
| C | PRO128 |
| C | GLY129 |
| C | SER130 |
| C | GLY132 |
| C | ALA133 |
| C | VAL136 |
| C | GLN137 |
| C | VAL139 |
| C | GLY140 |
| C | ALA141 |
| C | ARG176 |
| C | THR190 |
| C | VAL191 |
| C | VAL192 |
| C | ARG238 |
| C | SER254 |
| C | VAL255 |
| C | GLY256 |
| C | VAL363 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue K C 402 |
| Chain | Residue |
| C | VAL255 |
| C | SER257 |
| C | GLU361 |
| C | HOH567 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | binding site for residue FAD D 401 |
| Chain | Residue |
| D | THR26 |
| D | VAL65 |
| D | ALA67 |
| D | GLY68 |
| D | GLY69 |
| D | SER70 |
| D | ASN71 |
| D | LEU86 |
| D | ILE127 |
| D | PRO128 |
| D | GLY129 |
| D | SER130 |
| D | GLY132 |
| D | ALA133 |
| D | VAL136 |
| D | GLN137 |
| D | VAL139 |
| D | GLY140 |
| D | ALA141 |
| D | ARG176 |
| D | THR190 |
| D | VAL191 |
| D | VAL192 |
| D | ARG238 |
| D | SER254 |
| D | VAL255 |
| D | GLY256 |
| D | HOH509 |
| D | HOH528 |
| D | HOH548 |
| D | HOH562 |
| D | HOH570 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | binding site for residue FAD E 401 |
| Chain | Residue |
| E | THR26 |
| E | VAL65 |
| E | PHE66 |
| E | ALA67 |
| E | GLY68 |
| E | GLY69 |
| E | SER70 |
| E | ASN71 |
| E | LEU86 |
| E | PRO128 |
| E | GLY129 |
| E | SER130 |
| E | ALA133 |
| E | VAL136 |
| E | VAL139 |
| E | GLY140 |
| E | ALA141 |
| E | ARG176 |
| E | VAL188 |
| E | THR190 |
| E | VAL191 |
| E | VAL192 |
| E | ARG238 |
| E | MET243 |
| E | SER254 |
| E | VAL255 |
| E | GLY256 |
| E | HOH509 |
| site_id | AC9 |
| Number of Residues | 30 |
| Details | binding site for residue FAD F 401 |
| Chain | Residue |
| F | THR26 |
| F | VAL65 |
| F | PHE66 |
| F | ALA67 |
| F | GLY68 |
| F | GLY69 |
| F | SER70 |
| F | ASN71 |
| F | LEU72 |
| F | LEU86 |
| F | ILE127 |
| F | PRO128 |
| F | SER130 |
| F | GLY132 |
| F | ALA133 |
| F | VAL136 |
| F | VAL139 |
| F | GLY140 |
| F | ALA141 |
| F | ARG176 |
| F | GLY185 |
| F | VAL188 |
| F | THR190 |
| F | VAL191 |
| F | VAL192 |
| F | ARG238 |
| F | MET243 |
| F | SER254 |
| F | VAL255 |
| F | GLY256 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG176 | |
| A | GLU361 | |
| B | ARG176 | |
| B | GLU361 | |
| C | ARG176 | |
| C | GLU361 | |
| D | ARG176 | |
| D | GLU361 | |
| E | ARG176 | |
| E | GLU361 | |
| F | ARG176 | |
| F | GLU361 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton donor => ECO:0000250 |
| Chain | Residue | Details |
| A | SER257 | |
| B | SER257 | |
| C | SER257 | |
| D | SER257 | |
| E | SER257 | |
| F | SER257 |
