1ONL
Crystal structure of Thermus thermophilus HB8 H-protein of the glycine cleavage system
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005960 | cellular_component | glycine cleavage complex |
| A | 0009249 | biological_process | protein lipoylation |
| A | 0019464 | biological_process | glycine decarboxylation via glycine cleavage system |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005960 | cellular_component | glycine cleavage complex |
| B | 0009249 | biological_process | protein lipoylation |
| B | 0019464 | biological_process | glycine decarboxylation via glycine cleavage system |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005960 | cellular_component | glycine cleavage complex |
| C | 0009249 | biological_process | protein lipoylation |
| C | 0019464 | biological_process | glycine decarboxylation via glycine cleavage system |
Functional Information from PROSITE/UniProt
| site_id | PS00189 |
| Number of Residues | 30 |
| Details | LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GrvVekgEAVavVESvKTAsdIyapvaGeI |
| Chain | Residue | Details |
| A | GLY47-ILE76 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 246 |
| Details | Domain: {"description":"Lipoyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-lipoyllysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00272","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12925792","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






