1U7Z
Phosphopantothenoylcysteine synthetase from E. coli, 4'-phosphopantothenoyl-CMP complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004632 | molecular_function | phosphopantothenate--cysteine ligase activity |
| A | 0004633 | molecular_function | phosphopantothenoylcysteine decarboxylase activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0015937 | biological_process | coenzyme A biosynthetic process |
| A | 0015941 | biological_process | pantothenate catabolic process |
| B | 0004632 | molecular_function | phosphopantothenate--cysteine ligase activity |
| B | 0004633 | molecular_function | phosphopantothenoylcysteine decarboxylase activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0015937 | biological_process | coenzyme A biosynthetic process |
| B | 0015941 | biological_process | pantothenate catabolic process |
| C | 0004632 | molecular_function | phosphopantothenate--cysteine ligase activity |
| C | 0004633 | molecular_function | phosphopantothenoylcysteine decarboxylase activity |
| C | 0010181 | molecular_function | FMN binding |
| C | 0015937 | biological_process | coenzyme A biosynthetic process |
| C | 0015941 | biological_process | pantothenate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE PMT A 500 |
| Chain | Residue |
| A | SER212 |
| A | VAL277 |
| A | ASP279 |
| A | PRO308 |
| A | ASP309 |
| A | ILE310 |
| A | VAL311 |
| A | GLY326 |
| A | PHE327 |
| A | ALA329 |
| A | LYS341 |
| A | SER213 |
| A | LYS345 |
| A | ASN353 |
| A | GLY361 |
| A | PHE362 |
| A | ASN363 |
| A | LYS385 |
| A | HOH507 |
| A | HOH511 |
| A | HOH525 |
| A | HOH555 |
| A | GLY214 |
| B | LYS289 |
| A | LYS215 |
| A | MET216 |
| A | GLY273 |
| A | CYS274 |
| A | ALA275 |
| A | ALA276 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE PMT B 1500 |
| Chain | Residue |
| A | LYS289 |
| B | SER212 |
| B | SER213 |
| B | GLY214 |
| B | LYS215 |
| B | MET216 |
| B | GLY273 |
| B | CYS274 |
| B | ALA275 |
| B | ALA276 |
| B | VAL277 |
| B | ASP279 |
| B | PRO308 |
| B | ASP309 |
| B | ILE310 |
| B | VAL311 |
| B | GLY326 |
| B | PHE327 |
| B | ALA329 |
| B | LYS341 |
| B | LYS345 |
| B | ASN353 |
| B | PHE362 |
| B | ASN363 |
| B | LYS385 |
| B | HOH1508 |
| B | HOH1525 |
| B | HOH1535 |
| B | HOH1547 |
| B | HOH1564 |
| B | HOH1590 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE PMT C 2500 |
| Chain | Residue |
| C | SER212 |
| C | SER213 |
| C | GLY214 |
| C | LYS215 |
| C | MET216 |
| C | GLY273 |
| C | CYS274 |
| C | ALA275 |
| C | ALA276 |
| C | VAL277 |
| C | ASP279 |
| C | LYS289 |
| C | PRO308 |
| C | ASP309 |
| C | ILE310 |
| C | VAL311 |
| C | GLY326 |
| C | PHE327 |
| C | ALA329 |
| C | LYS341 |
| C | LYS345 |
| C | ASN353 |
| C | PHE362 |
| C | ASN363 |
| C | LYS385 |
| C | HOH2504 |
| C | HOH2506 |
| C | HOH2537 |
| C | HOH2572 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:15530362, ECO:0007744|PDB:1U7W |
| Chain | Residue | Details |
| A | CYS274 | |
| B | ILE290 | |
| B | ASP309 | |
| B | ALA328 | |
| B | ARG342 | |
| B | ASN346 | |
| C | CYS274 | |
| C | TYR280 | |
| C | ILE290 | |
| C | ASP309 | |
| C | ALA328 | |
| A | TYR280 | |
| C | ARG342 | |
| C | ASN346 | |
| A | ILE290 | |
| A | ASP309 | |
| A | ALA328 | |
| A | ARG342 | |
| A | ASN346 | |
| B | CYS274 | |
| B | TYR280 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1u7u |
| Chain | Residue | Details |
| A | ASP210 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1u7u |
| Chain | Residue | Details |
| B | ASP210 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1u7u |
| Chain | Residue | Details |
| C | ASP210 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 772 |
| Chain | Residue | Details |
| A | HIS211 | activator, electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 772 |
| Chain | Residue | Details |
| B | HIS211 | activator, electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 772 |
| Chain | Residue | Details |
| C | HIS211 | activator, electrostatic stabiliser |
