3R07
Structural analysis of an archaeal lipoylation system. A bi-partite lipoate protein ligase and its E2 lipoyl domain from Thermoplasma acidophilum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009249 | biological_process | protein lipoylation |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016979 | molecular_function | lipoate-protein ligase activity |
| A | 0017118 | molecular_function | lipoyltransferase activity |
| A | 0031405 | molecular_function | lipoic acid binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0036211 | biological_process | protein modification process |
| A | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0009249 | biological_process | protein lipoylation |
| C | 0016874 | molecular_function | ligase activity |
| C | 0016979 | molecular_function | lipoate-protein ligase activity |
| C | 0017118 | molecular_function | lipoyltransferase activity |
| C | 0032991 | cellular_component | protein-containing complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 263 |
| Chain | Residue |
| A | GLU9 |
| A | PHE38 |
| A | LEU86 |
| A | ARG211 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 264 |
| Chain | Residue |
| A | HIS161 |
| A | ARG72 |
| A | GLY77 |
| A | VAL79 |
| A | GLY148 |
| A | ALA149 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT C 89 |
| Chain | Residue |
| A | ARG227 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16141198","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ARU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16141198","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ART","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ARU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16141198","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16384580","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ARS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ART","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ARU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
