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6CZX

Crystal structure of Arabidopsis thaliana phosphoserine aminotransferase isoform 1 (AtPSAT1) in complex with PLP internal aldimine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004648molecular_functionO-phospho-L-serine:2-oxoglutarate aminotransferase activity
A0006564biological_processL-serine biosynthetic process
B0004648molecular_functionO-phospho-L-serine:2-oxoglutarate aminotransferase activity
B0006564biological_processL-serine biosynthetic process
C0004648molecular_functionO-phospho-L-serine:2-oxoglutarate aminotransferase activity
C0006564biological_processL-serine biosynthetic process
D0004648molecular_functionO-phospho-L-serine:2-oxoglutarate aminotransferase activity
D0006564biological_processL-serine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 501
ChainResidue
AGLY283
AASN284
ALYS296
AHOH612
AHOH733
AHOH869

site_idAC2
Number of Residues10
Detailsbinding site for residue SO4 A 502
ChainResidue
AHOH616
AHOH625
AHOH640
AHOH658
AHOH697
AHOH716
AHOH819
ALYS180
ALYS184
ATHR185

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 503
ChainResidue
ASER170
AASP173
ALYS192
ATYR196
AHOH677
AHOH767
AHOH850

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 504
ChainResidue
AASN86
ALEU318
AGLU321
AHOH604
AHOH732

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 A 505
ChainResidue
ALYS174
AHIS396
AARG397
AHOH605
AHOH877
AHOH907

site_idAC6
Number of Residues3
Detailsbinding site for residue PEG A 506
ChainResidue
AGLY236
AARG278
AHOH681

site_idAC7
Number of Residues6
Detailsbinding site for residue SO4 B 501
ChainResidue
BGLY283
BASN284
BLYS296
BHOH649
BHOH652
BHOH738

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 B 502
ChainResidue
AGLN392
BGLY112
BLYS113
BHOH645

site_idAC9
Number of Residues9
Detailsbinding site for residue PEG B 503
ChainResidue
BLYS228
BGLN337
BASP341
BLYS360
BSER361
BARG363
BLEU365
BHOH914
BHOH975

site_idAD1
Number of Residues6
Detailsbinding site for residue MRD B 504
ChainResidue
AHOH793
AHOH877
AHOH999
BHIS110
BARG111
BHOH741

site_idAD2
Number of Residues6
Detailsbinding site for residue SO4 C 501
ChainResidue
CGLY283
CASN284
CLYS296
CHOH630
CHOH634
CHOH673

site_idAD3
Number of Residues10
Detailsbinding site for residue SO4 C 502
ChainResidue
CLYS180
CLYS184
CTHR185
CHOH644
CHOH665
CHOH700
CHOH716
CHOH741
CHOH842
CHOH849

site_idAD4
Number of Residues6
Detailsbinding site for residue SO4 C 503
ChainResidue
CSER170
CASP173
CLYS192
CTYR196
CHOH768
CHOH774

site_idAD5
Number of Residues5
Detailsbinding site for residue SO4 C 504
ChainResidue
CLYS174
CHIS396
CARG397
CHOH607
CHOH766

site_idAD6
Number of Residues7
Detailsbinding site for residue PEG C 505
ChainResidue
CGLY236
CPHE237
CARG278
CHOH643
CHOH723
CHOH737
CHOH934

site_idAD7
Number of Residues8
Detailsbinding site for residue MRD C 506
ChainResidue
CHOH1039
DHIS396
DHOH723
DHOH943
DHOH982
CHIS110
CARG111
CHOH810

site_idAD8
Number of Residues6
Detailsbinding site for residue SO4 D 501
ChainResidue
DGLY283
DASN284
DLYS296
DHOH636
DHOH660
DHOH700

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues20
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. FGVIygGAQKnvgps.GvTiV
ChainResidueDetails
APHE256-VAL275

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG111
BARG111
CARG111
DARG111

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:30034403, ECO:0007744|PDB:6CZY, ECO:0007744|PDB:6CZZ
ChainResidueDetails
AALA145
BASN306
CALA145
CTHR221
CASP241
CGLN264
CASN306
DALA145
DTHR221
DASP241
DGLN264
ATHR221
DASN306
AASP241
AGLN264
AASN306
BALA145
BTHR221
BASP241
BGLN264

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:30034403, ECO:0007744|PDB:6CZZ
ChainResidueDetails
ATRP171
BTRP171
CTRP171
DTRP171

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:30034403, ECO:0007744|PDB:6CZY, ECO:0007744|PDB:6CZZ
ChainResidueDetails
ALLP265
BLLP265
CLLP265
DLLP265

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PDB entries from 2024-07-17

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