1U7W
Phosphopantothenoylcysteine synthetase from E. coli, CTP-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 | 4 |
Details | BINDING SITE FOR RESIDUE CA A 501 |
Chain | Residue |
A | ASP279 |
A | CTP500 |
A | HOH2502 |
A | HOH2503 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 1501 |
Chain | Residue |
A | LYS289 |
B | ASP279 |
B | CTP1500 |
B | HOH2504 |
B | HOH2505 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA C 2501 |
Chain | Residue |
C | ASP279 |
C | CTP2500 |
C | HOH2506 |
C | HOH2507 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CTP A 500 |
Chain | Residue |
A | HOH32 |
A | GLY273 |
A | ALA275 |
A | VAL277 |
A | ASP279 |
A | PRO308 |
A | ASP309 |
A | ILE310 |
A | VAL311 |
A | GLY326 |
A | PHE327 |
A | LYS341 |
A | LYS345 |
A | CA501 |
A | HOH2503 |
B | LYS289 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE CTP B 1500 |
Chain | Residue |
A | LYS289 |
B | HOH126 |
B | HOH138 |
B | GLY273 |
B | ALA275 |
B | VAL277 |
B | ASP279 |
B | PRO308 |
B | ASP309 |
B | ILE310 |
B | VAL311 |
B | GLY326 |
B | PHE327 |
B | LYS341 |
B | LYS345 |
B | CA1501 |
B | HOH2505 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CTP C 2500 |
Chain | Residue |
C | HOH68 |
C | HOH118 |
C | GLY273 |
C | ALA275 |
C | VAL277 |
C | ASP279 |
C | PRO308 |
C | ASP309 |
C | ILE310 |
C | VAL311 |
C | PHE327 |
C | LYS341 |
C | LYS345 |
C | CA2501 |
C | HOH2507 |
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 |