1JYL
Catalytic Mechanism of CTP:phosphocholine Cytidylyltransferase from Streptococcus pneumoniae (LicC)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019350 | biological_process | teichoic acid biosynthetic process |
| A | 0070395 | biological_process | lipoteichoic acid biosynthetic process |
| A | 0071555 | biological_process | cell wall organization |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019350 | biological_process | teichoic acid biosynthetic process |
| B | 0070395 | biological_process | lipoteichoic acid biosynthetic process |
| B | 0071555 | biological_process | cell wall organization |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0019350 | biological_process | teichoic acid biosynthetic process |
| C | 0070395 | biological_process | lipoteichoic acid biosynthetic process |
| C | 0071555 | biological_process | cell wall organization |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| D | 0019350 | biological_process | teichoic acid biosynthetic process |
| D | 0070395 | biological_process | lipoteichoic acid biosynthetic process |
| D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1996 |
| Chain | Residue |
| A | ASP107 |
| A | GLU216 |
| A | ASP218 |
| A | CDC1991 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 2996 |
| Chain | Residue |
| B | ASP107 |
| B | GLU216 |
| B | ASP218 |
| B | CDC2991 |
| B | HOH5164 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 3996 |
| Chain | Residue |
| C | ASP107 |
| C | GLU216 |
| C | ASP218 |
| C | CDC3991 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 4996 |
| Chain | Residue |
| D | ASP107 |
| D | GLU216 |
| D | ASP218 |
| D | CDC4991 |
| D | HOH5165 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CDC A 1991 |
| Chain | Residue |
| A | LEU11 |
| A | ALA12 |
| A | ALA13 |
| A | GLY14 |
| A | TYR82 |
| A | TYR85 |
| A | ASN86 |
| A | ASN87 |
| A | SER90 |
| A | ALA106 |
| A | ASP107 |
| A | TRP136 |
| A | TYR190 |
| A | ASP192 |
| A | GLU216 |
| A | ASP218 |
| A | MG1996 |
| A | HOH5004 |
| A | HOH5177 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE CDC B 2991 |
| Chain | Residue |
| A | PRO21 |
| B | LEU11 |
| B | ALA12 |
| B | ALA13 |
| B | GLY14 |
| B | LYS28 |
| B | TYR82 |
| B | TYR85 |
| B | ASN86 |
| B | ASN87 |
| B | SER90 |
| B | ALA106 |
| B | ASP107 |
| B | TRP136 |
| B | TYR190 |
| B | ASP192 |
| B | GLU216 |
| B | ASP218 |
| B | MG2996 |
| B | HOH5153 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CDC C 3991 |
| Chain | Residue |
| C | LEU11 |
| C | ALA12 |
| C | ALA13 |
| C | GLY14 |
| C | TYR82 |
| C | TYR85 |
| C | ASN86 |
| C | ASN87 |
| C | SER90 |
| C | ALA106 |
| C | ASP107 |
| C | TRP136 |
| C | TYR190 |
| C | ASP192 |
| C | GLU216 |
| C | ASP218 |
| C | MG3996 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE CDC D 4991 |
| Chain | Residue |
| C | PRO21 |
| C | GLU24 |
| D | LEU11 |
| D | ALA12 |
| D | ALA13 |
| D | GLY14 |
| D | LYS28 |
| D | TYR82 |
| D | TYR85 |
| D | ASN86 |
| D | ASN87 |
| D | SER90 |
| D | ALA106 |
| D | ASP107 |
| D | TRP136 |
| D | TYR190 |
| D | ASP192 |
| D | GLU216 |
| D | ASP218 |
| D | MG4996 |
| D | HOH5166 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11706035, ECO:0007744|PDB:1JYL |
| Chain | Residue | Details |
| A | LEU11 | |
| A | GLU216 | |
| A | ASP218 | |
| B | LEU11 | |
| B | ALA13 | |
| B | GLY14 | |
| B | TYR85 | |
| B | ASN87 | |
| B | SER90 | |
| B | ALA106 | |
| B | ASP107 | |
| A | ALA13 | |
| B | TYR190 | |
| B | GLU216 | |
| B | ASP218 | |
| C | LEU11 | |
| C | ALA13 | |
| C | GLY14 | |
| C | TYR85 | |
| C | ASN87 | |
| C | SER90 | |
| C | ALA106 | |
| A | GLY14 | |
| C | ASP107 | |
| C | TYR190 | |
| C | GLU216 | |
| C | ASP218 | |
| D | LEU11 | |
| D | ALA13 | |
| D | GLY14 | |
| D | TYR85 | |
| D | ASN87 | |
| D | SER90 | |
| A | TYR85 | |
| D | ALA106 | |
| D | ASP107 | |
| D | TYR190 | |
| D | GLU216 | |
| D | ASP218 | |
| A | ASN87 | |
| A | SER90 | |
| A | ALA106 | |
| A | ASP107 | |
| A | TYR190 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| A | ARG18 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| B | ARG18 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| C | ARG18 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| D | ARG18 |
