1U80
Phosphopantothenoylcysteine synthetase from E. coli, 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 | 9 |
Details | BINDING SITE FOR RESIDUE PO4 A 501 |
Chain | Residue |
A | HOH38 |
A | SER212 |
A | SER213 |
A | GLY214 |
A | LYS215 |
A | MET216 |
A | PHE362 |
A | ASN363 |
A | LYS385 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 B 1501 |
Chain | Residue |
B | SER212 |
B | SER213 |
B | GLY214 |
B | LYS215 |
B | MET216 |
B | PHE362 |
B | ASN363 |
B | LYS385 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 C 2501 |
Chain | Residue |
C | SER212 |
C | SER213 |
C | GLY214 |
C | LYS215 |
C | MET216 |
C | PHE362 |
C | ASN363 |
C | LYS385 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE C5P A 500 |
Chain | Residue |
A | HOH32 |
A | GLY273 |
A | ALA275 |
A | VAL277 |
A | PRO308 |
A | ASP309 |
A | ILE310 |
A | VAL311 |
A | GLY326 |
A | PHE327 |
A | LYS341 |
A | LYS345 |
B | LYS289 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE C5P B 1500 |
Chain | Residue |
A | LYS289 |
A | LYS292 |
B | GLY273 |
B | ALA275 |
B | VAL277 |
B | PRO308 |
B | ASP309 |
B | ILE310 |
B | VAL311 |
B | GLY326 |
B | PHE327 |
B | LYS341 |
B | LYS345 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE C5P C 2500 |
Chain | Residue |
C | GLY273 |
C | ALA275 |
C | VAL277 |
C | ASP279 |
C | LYS289 |
C | PRO308 |
C | ASP309 |
C | ILE310 |
C | VAL311 |
C | GLY326 |
C | PHE327 |
C | LYS341 |
C | LYS345 |
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 |