Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8FBZ

Crystal Structure of apo human Glutathione Synthetase Y270E

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004363molecular_functionglutathione synthase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0006750biological_processglutathione biosynthetic process
A0006979biological_processresponse to oxidative stress
A0007399biological_processnervous system development
A0016874molecular_functionligase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043295molecular_functionglutathione binding
A0046686biological_processresponse to cadmium ion
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
B0000287molecular_functionmagnesium ion binding
B0004363molecular_functionglutathione synthase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0006750biological_processglutathione biosynthetic process
B0006979biological_processresponse to oxidative stress
B0007399biological_processnervous system development
B0016874molecular_functionligase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043295molecular_functionglutathione binding
B0046686biological_processresponse to cadmium ion
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsBINDING:
ChainResidueDetails
BARG125
BGLU368
BTYR375
BMET398
BGLU425
BARG450
BLYS452
BASP458
BVAL461
AARG125
AGLU144
BGLU144
AASN146
AILE148
AGLU214
AGLN220
AARG267
ALYS305
ALYS364
AGLU368
ATYR375
AMET398
BASN146
AGLU425
AARG450
ALYS452
AASP458
AVAL461
BILE148
BGLU214
BGLN220
BARG267
BLYS305
BLYS364

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
BALA2
AALA2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER415
ASER415

Catalytic Information from CSA
site_idMCSA1
Number of Residues9
DetailsM-CSA 498
ChainResidueDetails
BARG125electrostatic stabiliser
BGLU144metal ligand
BASN146metal ligand
BSER151electrostatic stabiliser
BLYS305electrostatic stabiliser
BLYS364electrostatic stabiliser
BGLU368metal ligand
BGLY369electrostatic stabiliser
BARG450electrostatic stabiliser

site_idMCSA2
Number of Residues9
DetailsM-CSA 498
ChainResidueDetails
AARG125electrostatic stabiliser
AGLU144metal ligand
AASN146metal ligand
ASER151electrostatic stabiliser
ALYS305electrostatic stabiliser
ALYS364electrostatic stabiliser
AGLU368metal ligand
AGLY369electrostatic stabiliser
AARG450electrostatic stabiliser

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon