Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0005654 | cellular_component | nucleoplasm |
| 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 | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | GLU144 |
| A | ASN146 |
| A | GLU368 |
| A | ADP500 |
| A | MG502 |
| A | SO4505 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| A | SO4505 |
| A | HOH622 |
| A | HOH735 |
| A | GLU144 |
| A | ADP500 |
| A | MG501 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 504 |
| Chain | Residue |
| A | LYS384 |
| A | LEU410 |
| A | ARG412 |
| A | ARG418 |
| A | ALA453 |
| A | HIS456 |
| A | HOH512 |
| A | HOH552 |
| A | HOH640 |
| A | HOH642 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | ARG125 |
| A | GLU144 |
| A | ASN146 |
| A | GLU368 |
| A | GLY369 |
| A | ARG450 |
| A | ADP500 |
| A | MG501 |
| A | MG502 |
| A | GSH503 |
| A | HOH622 |
| A | HOH623 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE ADP A 500 |
| Chain | Residue |
| A | ILE143 |
| A | GLU144 |
| A | LYS305 |
| A | LYS364 |
| A | GLU368 |
| A | GLY369 |
| A | GLY370 |
| A | ASN373 |
| A | TYR375 |
| A | MET398 |
| A | GLU399 |
| A | LYS400 |
| A | ILE401 |
| A | GLU425 |
| A | LYS452 |
| A | ALA457 |
| A | ASP458 |
| A | GLY459 |
| A | MG501 |
| A | MG502 |
| A | SO4505 |
| A | HOH510 |
| A | HOH528 |
| A | HOH621 |
| A | HOH622 |
| A | HOH623 |
| A | HOH625 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE GSH A 503 |
| Chain | Residue |
| A | ARG125 |
| A | ILE148 |
| A | SER149 |
| A | ALA150 |
| A | SER151 |
| A | PHE152 |
| A | GLU214 |
| A | ASN216 |
| A | GLN220 |
| A | ARG267 |
| A | TYR270 |
| A | ARG450 |
| A | GLY460 |
| A | VAL461 |
| A | ALA462 |
| A | SO4505 |
| A | HOH520 |
| A | HOH557 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 8445637, 10369661 |
| Chain | Residue | Details |
| A | SER151 | |
| A | GLY369 | |
| A | ARG125 | |
| A | ARG450 | |
| site_id | MCSA1 |
| 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 |
