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 | 0005654 | cellular_component | nucleoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005886 | cellular_component | plasma membrane |
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 |
A | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
B | 0004375 | molecular_function | glycine dehydrogenase (decarboxylating) activity |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005886 | cellular_component | plasma membrane |
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 |
B | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
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 | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q91W43 |
Chain | Residue | Details |
A | LYS447 | |
A | LYS514 | |
A | LYS648 | |
A | LYS664 | |
B | LYS447 | |
B | LYS514 | |
B | LYS648 | |
B | LYS664 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:P15505 |
Chain | Residue | Details |
A | LYS754 | |
B | LYS754 |