3A7A
Crystal structure of E. coli lipoate-protein ligase A in complex with octyl-amp and apoH-protein
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0036211 | biological_process | protein modification process |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005960 | cellular_component | glycine cleavage complex |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0019464 | biological_process | glycine decarboxylation via glycine cleavage system |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| 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 | 0036211 | biological_process | protein modification process |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0005960 | cellular_component | glycine cleavage complex |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0019464 | biological_process | glycine decarboxylation via glycine cleavage system |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OCT A 401 |
| Chain | Residue |
| A | TRP37 |
| A | ARG70 |
| A | GLY75 |
| A | VAL77 |
| A | AMP402 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AMP A 402 |
| Chain | Residue |
| A | LYS133 |
| A | THR151 |
| A | LEU153 |
| A | LEU165 |
| A | VAL180 |
| A | ARG181 |
| A | SER182 |
| A | OCT401 |
| A | GLY75 |
| A | VAL77 |
| A | PHE78 |
| A | ASN83 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OCT C 401 |
| Chain | Residue |
| C | ARG70 |
| C | GLY75 |
| C | VAL77 |
| C | SER137 |
| C | HIS149 |
| C | AMP402 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AMP C 402 |
| Chain | Residue |
| C | GLY75 |
| C | ALA76 |
| C | VAL77 |
| C | PHE78 |
| C | ASN83 |
| C | LYS133 |
| C | THR151 |
| C | LEU153 |
| C | LEU165 |
| C | VAL180 |
| C | SER182 |
| C | VAL184 |
| C | OCT401 |
Functional Information from PROSITE/UniProt
| site_id | PS00189 |
| Number of Residues | 30 |
| Details | LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GatVsagDDCavAESvKAAsdIyapvsGeI |
| Chain | Residue | Details |
| B | GLY48-ILE77 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 374 |
| Details | Domain: {"description":"BPL/LPL catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01067","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 164 |
| Details | Domain: {"description":"Lipoyl-binding","evidences":[{"source":"HAMAP-Rule","id":"MF_00272","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-lipoyllysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00272","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
