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2ISQ

Crystal Structure of O-Acetylserine Sulfhydrylase from Arabidopsis Thaliana in Complex with C-Terminal Peptide from Arabidopsis Serine Acetyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000325cellular_componentplant-type vacuole
A0003729molecular_functionmRNA binding
A0004124molecular_functioncysteine synthase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006535biological_processcysteine biosynthetic process from serine
A0007568biological_processobsolete aging
A0009507cellular_componentchloroplast
A0009567biological_processdouble fertilization forming a zygote and endosperm
A0009570cellular_componentchloroplast stroma
A0009860biological_processpollen tube growth
A0016740molecular_functiontransferase activity
A0019344biological_processcysteine biosynthetic process
A0046686biological_processresponse to cadmium ion
A0048046cellular_componentapoplast
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 500
ChainResidue
ATHR305
AVAL306

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP A 400
ChainResidue
ATHR185
AGLY225
ASER269
APRO296
ASER297
ATYR302
AHOH503
AHOH565
BHOH6
ALYS46
AASN77
AGLY179
AILE180
AGLY181
ATHR182
AGLY183

Functional Information from PROSITE/UniProt
site_idPS00901
Number of Residues19
DetailsCYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KlEmme.PCsSVKdRiGfsM
ChainResidueDetails
ALYS35-MET53

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16166087, ECO:0000269|PubMed:17194764, ECO:0007744|PDB:1Z7W, ECO:0007744|PDB:2ISQ
ChainResidueDetails
AASN77
AGLY181
ASER269

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:16166087, ECO:0000269|PubMed:17194764, ECO:0007744|PDB:1Z7W, ECO:0007744|PDB:2ISQ
ChainResidueDetails
ALYS46

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22092075
ChainResidueDetails
ASER178

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1oas
ChainResidueDetails
ASER269
ALYS46

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oas
ChainResidueDetails
ALYS46

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1oas
ChainResidueDetails
ALYS46
ASER297

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PDB entries from 2024-07-24

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