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 |