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 |
| B | 0005960 | cellular_component | glycine cleavage complex |
| B | 0019464 | biological_process | glycine decarboxylation via glycine cleavage system |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE RED A 163 |
| Chain | Residue |
| A | HIS34 |
| A | LEU35 |
| A | LYS63 |
| A | GLU127 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE RED B 163 |
| Chain | Residue |
| B | LYS63 |
| A | SER21 |
| A | VAL22 |
| A | GLU78 |
| A | LYS102 |
| B | HIS34 |
Functional Information from PROSITE/UniProt
| site_id | PS00189 |
| Number of Residues | 30 |
| Details | LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GvsVtkgKGFgaVESvKATsdVnspisGeV |
| Chain | Residue | Details |
| A | GLY47-VAL76 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 164 |
| Details | Domain: {"description":"Lipoyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-lipoyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2363710","evidenceCode":"ECO:0000269"}]} |
