4JAY
Crystal structure of P. aeruginosa MurB in complex with NADP+
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD A 1001 |
| Chain | Residue |
| A | VAL51 |
| A | PRO118 |
| A | GLY119 |
| A | THR120 |
| A | ALA123 |
| A | MET126 |
| A | GLN127 |
| A | ILE129 |
| A | GLY130 |
| A | ALA131 |
| A | TRP177 |
| A | GLY53 |
| A | ILE179 |
| A | ARG224 |
| A | ASN236 |
| A | GLY238 |
| A | ASN337 |
| A | NAP1002 |
| A | HOH1104 |
| A | HOH1111 |
| A | HOH1123 |
| A | HOH1130 |
| A | GLY54 |
| A | HOH1150 |
| A | GLY55 |
| A | SER56 |
| A | ASN57 |
| A | LEU58 |
| A | MET71 |
| A | ILE117 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAP A 1002 |
| Chain | Residue |
| A | ALA131 |
| A | TYR132 |
| A | ARG166 |
| A | ASP195 |
| A | TYR196 |
| A | LYS227 |
| A | GLY238 |
| A | SER239 |
| A | ASN243 |
| A | TYR264 |
| A | LYS272 |
| A | GLU335 |
| A | FAD1001 |
| A | K1004 |
| A | HOH1139 |
| A | HOH1143 |
| A | HOH1157 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE B3P A 1003 |
| Chain | Residue |
| A | GLY133 |
| A | VAL134 |
| A | GLU135 |
| A | ASP138 |
| A | HIS193 |
| A | ASP195 |
| A | HOH1153 |
| A | HOH1171 |
| C | GLY282 |
| C | GLY283 |
| C | TRP284 |
| C | PHE287 |
| C | ARG319 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 1004 |
| Chain | Residue |
| A | ASN57 |
| A | ALA237 |
| A | SER239 |
| A | GLU335 |
| A | NAP1002 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 401 |
| Chain | Residue |
| B | ASN57 |
| B | ALA237 |
| B | SER239 |
| B | GLU335 |
| B | FAD402 |
| B | NAP403 |
| site_id | AC6 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD B 402 |
| Chain | Residue |
| B | HOH528 |
| B | HOH532 |
| B | VAL51 |
| B | GLY53 |
| B | GLY54 |
| B | GLY55 |
| B | SER56 |
| B | ASN57 |
| B | LEU58 |
| B | MET71 |
| B | ILE117 |
| B | PRO118 |
| B | GLY119 |
| B | THR120 |
| B | ALA123 |
| B | MET126 |
| B | GLN127 |
| B | ILE129 |
| B | GLY130 |
| B | ALA131 |
| B | TRP177 |
| B | ILE179 |
| B | ARG224 |
| B | ASN236 |
| B | ALA237 |
| B | GLY238 |
| B | ASN337 |
| B | K401 |
| B | NAP403 |
| B | HOH505 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAP B 403 |
| Chain | Residue |
| B | ALA131 |
| B | TYR132 |
| B | TYR165 |
| B | ARG166 |
| B | TYR196 |
| B | LYS227 |
| B | LEU228 |
| B | GLY238 |
| B | SER239 |
| B | ASN243 |
| B | TYR264 |
| B | LYS272 |
| B | GLN298 |
| B | GLU335 |
| B | K401 |
| B | FAD402 |
| B | HOH562 |
| B | HOH568 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE B3P B 404 |
| Chain | Residue |
| A | GLY282 |
| A | GLY283 |
| A | TRP284 |
| A | PHE287 |
| B | GLY133 |
| B | VAL134 |
| B | GLU135 |
| B | ASP138 |
| B | HIS193 |
| B | ASP195 |
| B | HOH544 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 401 |
| Chain | Residue |
| C | ASN57 |
| C | ALA237 |
| C | SER239 |
| C | GLU335 |
| C | FAD402 |
| C | NAP403 |
| site_id | BC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD C 402 |
| Chain | Residue |
| C | VAL51 |
| C | ILE52 |
| C | GLY53 |
| C | GLY54 |
| C | GLY55 |
| C | SER56 |
| C | ASN57 |
| C | LEU58 |
| C | MET71 |
| C | ILE117 |
| C | PRO118 |
| C | GLY119 |
| C | THR120 |
| C | ALA123 |
| C | MET126 |
| C | GLN127 |
| C | ILE129 |
| C | GLY130 |
| C | ALA131 |
| C | TRP177 |
| C | ILE179 |
| C | ARG224 |
| C | ASN236 |
| C | ALA237 |
| C | GLY238 |
| C | ASN337 |
| C | K401 |
| C | NAP403 |
| C | HOH501 |
| C | HOH505 |
| C | HOH527 |
| C | HOH576 |
| site_id | BC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAP C 403 |
| Chain | Residue |
| C | ALA131 |
| C | TYR132 |
| C | ARG166 |
| C | TYR196 |
| C | LYS227 |
| C | GLY238 |
| C | SER239 |
| C | ASN243 |
| C | TYR264 |
| C | LYS272 |
| C | GLN298 |
| C | GLU335 |
| C | K401 |
| C | FAD402 |
| C | HOH524 |
| C | HOH528 |
| C | HOH536 |
| C | HOH547 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE B3P C 404 |
| Chain | Residue |
| C | GLY133 |
| C | VAL134 |
| C | ASP138 |
| C | HIS193 |
| C | ASP195 |
| C | HOH548 |
| D | GLY282 |
| D | TRP284 |
| D | PHE287 |
| D | ARG319 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D 401 |
| Chain | Residue |
| D | ASN57 |
| D | ALA237 |
| D | SER239 |
| D | GLU335 |
| D | FAD402 |
| D | NAP403 |
| site_id | BC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD D 402 |
| Chain | Residue |
| D | VAL51 |
| D | ILE52 |
| D | GLY53 |
| D | GLY54 |
| D | GLY55 |
| D | SER56 |
| D | ASN57 |
| D | LEU58 |
| D | MET71 |
| D | ILE117 |
| D | PRO118 |
| D | GLY119 |
| D | THR120 |
| D | ALA123 |
| D | MET126 |
| D | GLN127 |
| D | ILE129 |
| D | GLY130 |
| D | ALA131 |
| D | TRP177 |
| D | ILE179 |
| D | ARG224 |
| D | ASN236 |
| D | ALA237 |
| D | GLY238 |
| D | ASN337 |
| D | K401 |
| D | NAP403 |
| D | HOH503 |
| D | HOH508 |
| D | HOH518 |
| D | HOH566 |
| site_id | BC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP D 403 |
| Chain | Residue |
| D | ALA131 |
| D | TYR132 |
| D | ARG166 |
| D | ASP195 |
| D | TYR196 |
| D | LYS227 |
| D | GLY238 |
| D | SER239 |
| D | ASN243 |
| D | TYR264 |
| D | LYS272 |
| D | GLU335 |
| D | K401 |
| D | FAD402 |
| D | HOH532 |
| D | HOH533 |
| D | HOH545 |
| D | HOH558 |
| D | HOH561 |
| site_id | BC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE B3P D 404 |
| Chain | Residue |
| B | GLY282 |
| B | GLY283 |
| B | TRP284 |
| B | PHE287 |
| D | GLY133 |
| D | VAL134 |
| D | GLU135 |
| D | ASP138 |
| D | HIS193 |
| D | ASP195 |
| D | HOH569 |
Functional Information from PROSITE/UniProt
| site_id | PS00430 |
| Number of Residues | 92 |
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. smslelqehcslkpyntfgidvrarllahardeadvrealalarerglpllvigggsnllltrdvealvlrmasqgrrivsdaa...............................DSVLVEAE |
| Chain | Residue | Details |
| A | SER0-GLU91 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00037 |
| Chain | Residue | Details |
| A | ARG166 | |
| A | GLU335 | |
| B | ARG166 | |
| B | GLU335 | |
| C | ARG166 | |
| C | GLU335 | |
| D | ARG166 | |
| D | GLU335 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00037 |
| Chain | Residue | Details |
| A | SER239 | |
| B | SER239 | |
| C | SER239 | |
| D | SER239 |
