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5OES

The structure of a glutathione synthetase (StGSS1) from Solanum tuberosum in ADP and y-EC bound closed conformation.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004363molecular_functionglutathione synthase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006750biological_processglutathione biosynthetic process
A0016874molecular_functionligase activity
A0043295molecular_functionglutathione binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004363molecular_functionglutathione synthase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006750biological_processglutathione biosynthetic process
B0016874molecular_functionligase activity
B0043295molecular_functionglutathione binding
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0004363molecular_functionglutathione synthase activity
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006750biological_processglutathione biosynthetic process
C0016874molecular_functionligase activity
C0043295molecular_functionglutathione binding
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0004363molecular_functionglutathione synthase activity
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0006750biological_processglutathione biosynthetic process
D0016874molecular_functionligase activity
D0043295molecular_functionglutathione binding
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0000287molecular_functionmagnesium ion binding
E0004363molecular_functionglutathione synthase activity
E0005524molecular_functionATP binding
E0005829cellular_componentcytosol
E0006750biological_processglutathione biosynthetic process
E0016874molecular_functionligase activity
E0043295molecular_functionglutathione binding
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0000287molecular_functionmagnesium ion binding
F0004363molecular_functionglutathione synthase activity
F0005524molecular_functionATP binding
F0005829cellular_componentcytosol
F0006750biological_processglutathione biosynthetic process
F0016874molecular_functionligase activity
F0043295molecular_functionglutathione binding
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue ADP A 501
ChainResidue
AMET141
AARG410
AILE411
AGLU434
ALYS461
AMG504
AILE152
AGLU153
ALYS318
ALYS372
AASN381
ATYR383
AMET408
AGLN409

site_idAC2
Number of Residues10
Detailsbinding site for residue 3GC A 502
ChainResidue
AARG137
AASN155
AILE157
ASER158
ASER160
AGLU225
AASN227
AGLN231
AARG279
ATYR282

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 503
ChainResidue
ALEU154
AGLY316
AHOH666

site_idAC4
Number of Residues5
Detailsbinding site for residue MG A 504
ChainResidue
AASP139
AGLU153
AGLU434
AARG459
AADP501

site_idAC5
Number of Residues11
Detailsbinding site for residue ADP B 501
ChainResidue
BMET141
BGLU153
BLYS372
BASN381
BTYR383
BMET408
BGLN409
BARG410
BILE411
BGLU434
BLYS461

site_idAC6
Number of Residues10
Detailsbinding site for residue 3GC B 502
ChainResidue
BARG137
BASN155
BILE157
BSER158
BSER160
BGLU225
BASN227
BGLN231
BARG279
BTYR282

site_idAC7
Number of Residues3
Detailsbinding site for residue MG B 503
ChainResidue
BLEU154
BGLY316
BHOH655

site_idAC8
Number of Residues16
Detailsbinding site for residue ADP C 501
ChainResidue
CMET141
CILE152
CGLU153
CLYS318
CVAL370
CLYS372
CASN381
CTYR383
CMET408
CGLN409
CARG410
CILE411
CGLU434
CLYS461
CMG504
CHOH629

site_idAC9
Number of Residues10
Detailsbinding site for residue 3GC C 502
ChainResidue
CARG137
CASN155
CILE157
CSER158
CSER160
CGLU225
CASN227
CGLN231
CARG279
CTYR282

site_idAD1
Number of Residues4
Detailsbinding site for residue MG C 503
ChainResidue
CLEU154
CGLY316
CHOH616
CHOH634

site_idAD2
Number of Residues5
Detailsbinding site for residue MG C 504
ChainResidue
CASP139
CGLU153
CGLU434
CARG459
CADP501

site_idAD3
Number of Residues13
Detailsbinding site for residue ADP D 501
ChainResidue
DARG410
DILE411
DGLU434
DLYS461
DMG503
DMET141
DGLU153
DVAL370
DLYS372
DASN381
DTYR383
DMET408
DGLN409

site_idAD4
Number of Residues10
Detailsbinding site for residue 3GC D 502
ChainResidue
DARG137
DASN155
DILE157
DSER158
DSER160
DGLU225
DASN227
DGLN231
DARG279
DTYR282

site_idAD5
Number of Residues5
Detailsbinding site for residue MG D 503
ChainResidue
DASP139
DGLU153
DGLU434
DARG459
DADP501

site_idAD6
Number of Residues3
Detailsbinding site for residue MG D 504
ChainResidue
DLEU154
DGLY316
DHOH629

site_idAD7
Number of Residues13
Detailsbinding site for residue ADP E 501
ChainResidue
EMET141
EGLU153
ELYS372
EGLU376
EASN381
ETYR383
EMET408
EGLN409
EARG410
EILE411
EGLU434
ELYS461
EHOH632

site_idAD8
Number of Residues10
Detailsbinding site for residue 3GC E 502
ChainResidue
EARG137
EASN155
EILE157
ESER158
ESER160
EGLU225
EASN227
EGLN231
EARG279
ETYR282

site_idAD9
Number of Residues4
Detailsbinding site for residue MG E 503
ChainResidue
ELEU154
EGLY316
EGLU376
EHOH651

site_idAE1
Number of Residues4
Detailsbinding site for residue MG E 504
ChainResidue
EASP139
EGLU153
EGLU434
EARG459

site_idAE2
Number of Residues13
Detailsbinding site for residue ADP F 501
ChainResidue
FMET141
FILE152
FGLU153
FLYS318
FLYS372
FASN381
FTYR383
FMET408
FGLN409
FILE411
FGLU434
FLYS461
FHOH621

site_idAE3
Number of Residues10
Detailsbinding site for residue 3GC F 502
ChainResidue
FARG137
FASN155
FILE157
FSER158
FSER160
FGLU225
FASN227
FGLN231
FARG279
FTYR282

site_idAE4
Number of Residues4
Detailsbinding site for residue MG F 503
ChainResidue
FLEU154
FGLY316
FGLN321
FHOH642

218853

PDB entries from 2024-04-24

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