8FBZ
Crystal Structure of apo human Glutathione Synthetase Y270E
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004363 | molecular_function | glutathione synthase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0006750 | biological_process | glutathione biosynthetic process |
A | 0006979 | biological_process | response to oxidative stress |
A | 0007399 | biological_process | nervous system development |
A | 0016874 | molecular_function | ligase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0043295 | molecular_function | glutathione binding |
A | 0046686 | biological_process | response to cadmium ion |
A | 0046872 | molecular_function | metal ion binding |
A | 0070062 | cellular_component | extracellular exosome |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004363 | molecular_function | glutathione synthase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0006750 | biological_process | glutathione biosynthetic process |
B | 0006979 | biological_process | response to oxidative stress |
B | 0007399 | biological_process | nervous system development |
B | 0016874 | molecular_function | ligase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0043295 | molecular_function | glutathione binding |
B | 0046686 | biological_process | response to cadmium ion |
B | 0046872 | molecular_function | metal ion binding |
B | 0070062 | cellular_component | extracellular exosome |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 34 |
Details | BINDING: |
Chain | Residue | Details |
B | ARG125 | |
B | GLU368 | |
B | TYR375 | |
B | MET398 | |
B | GLU425 | |
B | ARG450 | |
B | LYS452 | |
B | ASP458 | |
B | VAL461 | |
A | ARG125 | |
A | GLU144 | |
B | GLU144 | |
A | ASN146 | |
A | ILE148 | |
A | GLU214 | |
A | GLN220 | |
A | ARG267 | |
A | LYS305 | |
A | LYS364 | |
A | GLU368 | |
A | TYR375 | |
A | MET398 | |
B | ASN146 | |
A | GLU425 | |
A | ARG450 | |
A | LYS452 | |
A | ASP458 | |
A | VAL461 | |
B | ILE148 | |
B | GLU214 | |
B | GLN220 | |
B | ARG267 | |
B | LYS305 | |
B | LYS364 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895 |
Chain | Residue | Details |
B | ALA2 | |
A | ALA2 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
B | SER415 | |
A | SER415 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 9 |
Details | M-CSA 498 |
Chain | Residue | Details |
B | ARG125 | electrostatic stabiliser |
B | GLU144 | metal ligand |
B | ASN146 | metal ligand |
B | SER151 | electrostatic stabiliser |
B | LYS305 | electrostatic stabiliser |
B | LYS364 | electrostatic stabiliser |
B | GLU368 | metal ligand |
B | GLY369 | electrostatic stabiliser |
B | ARG450 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 9 |
Details | M-CSA 498 |
Chain | Residue | Details |
A | ARG125 | electrostatic stabiliser |
A | GLU144 | metal ligand |
A | ASN146 | metal ligand |
A | SER151 | electrostatic stabiliser |
A | LYS305 | electrostatic stabiliser |
A | LYS364 | electrostatic stabiliser |
A | GLU368 | metal ligand |
A | GLY369 | electrostatic stabiliser |
A | ARG450 | electrostatic stabiliser |