6I33
Crystal structure of human glycine decarboxylase (P-protein)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004375 | molecular_function | glycine dehydrogenase (decarboxylating) activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005960 | cellular_component | glycine cleavage complex |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006544 | biological_process | glycine metabolic process |
| A | 0006546 | biological_process | glycine catabolic process |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016594 | molecular_function | glycine binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019464 | biological_process | glycine decarboxylation via glycine cleavage system |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0036255 | biological_process | response to methylamine |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0070280 | molecular_function | pyridoxal binding |
| A | 1903442 | biological_process | response to lipoic acid |
| B | 0004375 | molecular_function | glycine dehydrogenase (decarboxylating) activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005960 | cellular_component | glycine cleavage complex |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006544 | biological_process | glycine metabolic process |
| B | 0006546 | biological_process | glycine catabolic process |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016594 | molecular_function | glycine binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019464 | biological_process | glycine decarboxylation via glycine cleavage system |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0036255 | biological_process | response to methylamine |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0070280 | molecular_function | pyridoxal binding |
| B | 1903442 | biological_process | response to lipoic acid |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue PLP A 1101 |
| Chain | Residue |
| A | CYS382 |
| A | ASP727 |
| A | ALA729 |
| A | ASN751 |
| A | HIS753 |
| A | LYS754 |
| A | HOH1209 |
| A | THR383 |
| A | SER557 |
| A | SER617 |
| A | GLY618 |
| A | ALA619 |
| A | GLU622 |
| A | HIS651 |
| A | THR653 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 1102 |
| Chain | Residue |
| A | TRP130 |
| A | ASP586 |
| A | GLN587 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 1103 |
| Chain | Residue |
| A | ARG66 |
| A | GLU113 |
| A | HOH1203 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 1104 |
| Chain | Residue |
| A | SER649 |
| A | ILE676 |
| A | ILE697 |
| A | THR698 |
| A | SER701 |
| A | THR702 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 1105 |
| Chain | Residue |
| A | ILE129 |
| A | ASN140 |
| A | LYS574 |
| A | ASN578 |
| A | EDO1106 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 1106 |
| Chain | Residue |
| A | ASN140 |
| A | CYS141 |
| A | SER142 |
| A | VAL143 |
| A | EDO1105 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue BCT A 1107 |
| Chain | Residue |
| A | ARG461 |
| A | LEU462 |
| A | PHE582 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue PLP B 1101 |
| Chain | Residue |
| B | CYS382 |
| B | THR383 |
| B | SER557 |
| B | SER617 |
| B | GLY618 |
| B | ALA619 |
| B | GLU622 |
| B | HIS651 |
| B | THR653 |
| B | ASP727 |
| B | ALA729 |
| B | ASN751 |
| B | HIS753 |
| B | LYS754 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 1102 |
| Chain | Residue |
| A | LYS981 |
| A | PHE982 |
| B | ASN543 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 1103 |
| Chain | Residue |
| B | ARG66 |
| B | GLU113 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 1104 |
| Chain | Residue |
| A | TRP573 |
| B | GLN145 |
| B | LEU148 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 1105 |
| Chain | Residue |
| B | CYS141 |
| B | VAL143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91W43","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"P15505","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
