3WDL
Crystal structure of 4-phosphopantoate-beta-alanine ligase complexed with ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0015937 | biological_process | coenzyme A biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016881 | molecular_function | acid-amino acid ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0015937 | biological_process | coenzyme A biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0016881 | molecular_function | acid-amino acid ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0015937 | biological_process | coenzyme A biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| C | 0016881 | molecular_function | acid-amino acid ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0015937 | biological_process | coenzyme A biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
| D | 0016881 | molecular_function | acid-amino acid ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP A 900 |
| Chain | Residue |
| A | ALA36 |
| A | SER188 |
| A | ASP198 |
| A | ASN199 |
| A | ILE200 |
| A | HOH1001 |
| A | HOH1014 |
| A | ARG39 |
| A | LEU161 |
| A | GLY164 |
| A | ASP181 |
| A | LEU182 |
| A | ASN183 |
| A | SER186 |
| A | ARG187 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ATP B 901 |
| Chain | Residue |
| A | ARG17 |
| A | TYR45 |
| B | ALA36 |
| B | ARG39 |
| B | LEU83 |
| B | LEU161 |
| B | ASP163 |
| B | GLY164 |
| B | ASP181 |
| B | LEU182 |
| B | ASN183 |
| B | SER186 |
| B | ARG187 |
| B | SER188 |
| B | ASP198 |
| B | ASN199 |
| B | ILE200 |
| B | MG902 |
| B | HOH1006 |
| B | HOH1007 |
| B | HOH1015 |
| B | HOH1016 |
| B | HOH1019 |
| B | HOH1035 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 902 |
| Chain | Residue |
| B | ASP163 |
| B | ATP901 |
| B | HOH1025 |
| B | HOH1032 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP C 301 |
| Chain | Residue |
| C | ALA36 |
| C | ARG39 |
| C | LEU83 |
| C | LEU161 |
| C | GLU162 |
| C | ASP163 |
| C | ASP181 |
| C | LEU182 |
| C | ASN183 |
| C | SER186 |
| C | ARG187 |
| C | ASP198 |
| C | ASN199 |
| C | ILE200 |
| C | HOH411 |
| C | HOH412 |
| C | HOH415 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP D 301 |
| Chain | Residue |
| C | ARG17 |
| C | TYR45 |
| D | ALA36 |
| D | ARG39 |
| D | LEU83 |
| D | LEU161 |
| D | ASP163 |
| D | GLY164 |
| D | ASP181 |
| D | LEU182 |
| D | ASN183 |
| D | SER186 |
| D | ARG187 |
| D | SER188 |
| D | ASP198 |
| D | ASN199 |
| D | ILE200 |
| D | MG302 |
| D | HOH401 |
| D | HOH404 |
| D | HOH405 |
| D | HOH407 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 302 |
| Chain | Residue |
| D | ASP163 |
| D | ATP301 |
| D | HOH407 |
| D | HOH408 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:B6YXQ1, ECO:0000255|HAMAP-Rule:MF_02224 |
| Chain | Residue | Details |
| A | ARG17 | |
| B | ARG17 | |
| C | ARG17 | |
| D | ARG17 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000269|PubMed:24638914, ECO:0007744|PDB:3WDL |
| Chain | Residue | Details |
| A | ARG39 | |
| C | ASP181 | |
| C | ARG187 | |
| C | ASN199 | |
| D | ARG39 | |
| D | ASP181 | |
| D | ARG187 | |
| D | ASN199 | |
| A | ASP181 | |
| A | ARG187 | |
| A | ASN199 | |
| B | ARG39 | |
| B | ASP181 | |
| B | ARG187 | |
| B | ASN199 | |
| C | ARG39 |
