4H2T
Crystal structure of Bradyrhizobium japonicum glycine:[carrier protein] ligase complexed with cognate carrier protein and an analogue of glycyl adenylate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0016874 | molecular_function | ligase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0016874 | molecular_function | ligase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000035 | molecular_function | acyl binding |
| C | 0000036 | molecular_function | acyl carrier activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0009245 | biological_process | lipid A biosynthetic process |
| D | 0000035 | molecular_function | acyl binding |
| D | 0000036 | molecular_function | acyl carrier activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006633 | biological_process | fatty acid biosynthetic process |
| D | 0009245 | biological_process | lipid A biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1000 |
| Chain | Residue |
| A | CYS131 |
| A | GLU176 |
| A | CYS279 |
| A | G5A1001 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE G5A A 1001 |
| Chain | Residue |
| A | PHE172 |
| A | MET174 |
| A | GLU176 |
| A | LYS235 |
| A | ALA250 |
| A | CYS251 |
| A | MET252 |
| A | SER253 |
| A | ASN255 |
| A | CYS279 |
| A | ALA281 |
| A | GLY283 |
| A | ARG286 |
| A | ZN1000 |
| A | HOH1116 |
| A | HOH1155 |
| C | PNS1000 |
| A | ALA129 |
| A | CYS131 |
| A | ARG159 |
| A | GLU161 |
| A | LEU169 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | CYS131 |
| B | GLU176 |
| B | CYS279 |
| B | G5A402 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE G5A B 402 |
| Chain | Residue |
| B | CYS131 |
| B | ARG159 |
| B | GLU161 |
| B | LEU169 |
| B | PHE172 |
| B | MET174 |
| B | GLU176 |
| B | LYS235 |
| B | ALA250 |
| B | CYS251 |
| B | MET252 |
| B | SER253 |
| B | ASN255 |
| B | CYS279 |
| B | GLY283 |
| B | ARG286 |
| B | ZN401 |
| B | HOH520 |
| B | HOH540 |
| D | PNS1000 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 403 |
| Chain | Residue |
| A | PRO303 |
| B | SER118 |
| B | HOH503 |
| B | HOH504 |
| B | HOH561 |
| B | HOH563 |
| B | HOH593 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 404 |
| Chain | Residue |
| B | ARG66 |
| B | HOH542 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PNS C 1000 |
| Chain | Residue |
| A | TYR132 |
| A | ASP215 |
| A | PHE217 |
| A | GLN229 |
| A | HIS257 |
| A | HIS260 |
| A | G5A1001 |
| C | THR41 |
| C | SER42 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PNS D 1000 |
| Chain | Residue |
| B | TYR132 |
| B | ASP215 |
| B | PHE217 |
| B | GLN229 |
| B | GLN232 |
| B | HIS257 |
| B | ARG258 |
| B | HIS260 |
| B | G5A402 |
| B | HOH595 |
| D | SER42 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|PROSITE-ProRule:PRU00258 |
| Chain | Residue | Details |
| C | SER42 | |
| B | CYS131 | |
| B | ARG159 | |
| B | GLU161 | |
| B | ARG168 | |
| B | GLU176 | |
| B | LYS235 | |
| B | ALA250 | |
| B | CYS279 | |
| B | ARG286 | |
| D | SER42 | |
| A | GLU161 | |
| A | ARG168 | |
| A | GLU176 | |
| A | LYS235 | |
| A | ALA250 | |
| A | CYS279 | |
| A | ARG286 |
