Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005960 | cellular_component | glycine cleavage complex |
| A | 0019464 | biological_process | glycine decarboxylation via glycine cleavage system |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL A 201 |
| Chain | Residue |
| A | ASN25 |
| A | HOH432 |
| A | HOH466 |
| A | HOH467 |
| A | LYS59 |
| A | ALA60 |
| A | ASN87 |
| A | LYS88 |
| A | SER89 |
| A | CYS90 |
| A | HOH316 |
| A | HOH328 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 202 |
| Chain | Residue |
| A | ARG3 |
| A | LYS59 |
| A | GLU113 |
| A | HOH413 |
| A | HOH424 |
| A | HOH505 |
| A | HOH575 |
Functional Information from PROSITE/UniProt
| site_id | PS00189 |
| Number of Residues | 30 |
| Details | LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GtkLnkqEEFgaLESvKAAseLysplsGeV |
| Chain | Residue | Details |
| A | GLY43-VAL72 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 82 |
| Details | Domain: {"description":"Lipoyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-lipoyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2211640","evidenceCode":"ECO:0000269"}]} |