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5LNS

Crystal structure of Arabidopsis thaliana Pdx1-R5P complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006520biological_processamino acid metabolic process
A0006979biological_processresponse to oxidative stress
A0006982biological_processresponse to lipid hydroperoxide
A0009651biological_processresponse to salt stress
A0010224biological_processresponse to UV-B
A0010335biological_processresponse to non-ionic osmotic stress
A0012505cellular_componentendomembrane system
A0015994biological_processchlorophyll metabolic process
A0016829molecular_functionlyase activity
A0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
A0042538biological_processhyperosmotic salinity response
A0042803molecular_functionprotein homodimerization activity
A0042819biological_processvitamin B6 biosynthetic process
A0042823biological_processpyridoxal phosphate biosynthetic process
A0046982molecular_functionprotein heterodimerization activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006520biological_processamino acid metabolic process
B0006979biological_processresponse to oxidative stress
B0006982biological_processresponse to lipid hydroperoxide
B0009651biological_processresponse to salt stress
B0010224biological_processresponse to UV-B
B0010335biological_processresponse to non-ionic osmotic stress
B0012505cellular_componentendomembrane system
B0015994biological_processchlorophyll metabolic process
B0016829molecular_functionlyase activity
B0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
B0042538biological_processhyperosmotic salinity response
B0042803molecular_functionprotein homodimerization activity
B0042819biological_processvitamin B6 biosynthetic process
B0042823biological_processpyridoxal phosphate biosynthetic process
B0046982molecular_functionprotein heterodimerization activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006520biological_processamino acid metabolic process
C0006979biological_processresponse to oxidative stress
C0006982biological_processresponse to lipid hydroperoxide
C0009651biological_processresponse to salt stress
C0010224biological_processresponse to UV-B
C0010335biological_processresponse to non-ionic osmotic stress
C0012505cellular_componentendomembrane system
C0015994biological_processchlorophyll metabolic process
C0016829molecular_functionlyase activity
C0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
C0042538biological_processhyperosmotic salinity response
C0042803molecular_functionprotein homodimerization activity
C0042819biological_processvitamin B6 biosynthetic process
C0042823biological_processpyridoxal phosphate biosynthetic process
C0046982molecular_functionprotein heterodimerization activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006520biological_processamino acid metabolic process
D0006979biological_processresponse to oxidative stress
D0006982biological_processresponse to lipid hydroperoxide
D0009651biological_processresponse to salt stress
D0010224biological_processresponse to UV-B
D0010335biological_processresponse to non-ionic osmotic stress
D0012505cellular_componentendomembrane system
D0015994biological_processchlorophyll metabolic process
D0016829molecular_functionlyase activity
D0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
D0042538biological_processhyperosmotic salinity response
D0042803molecular_functionprotein homodimerization activity
D0042819biological_processvitamin B6 biosynthetic process
D0042823biological_processpyridoxal phosphate biosynthetic process
D0046982molecular_functionprotein heterodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue PO4 A 402
ChainResidue
AHIS132
AGLU151
AARG154
AARG155
AHOH506
AHOH588
AHOH672
DLYS204
DHOH616

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 B 402
ChainResidue
BHIS132
BARG154
BARG155
BHOH584
BHOH679
CLYS204

site_idAC3
Number of Residues6
Detailsbinding site for residue PO4 C 402
ChainResidue
BLYS204
CHIS132
CGLU151
CARG154
CARG155
CHOH617

site_idAC4
Number of Residues7
Detailsbinding site for residue PO4 D 402
ChainResidue
ALYS204
DHIS132
DARG154
DARG155
DHOH572
DHOH586
DHOH619

site_idAC5
Number of Residues27
Detailsbinding site for Poly-Saccharide residues LYS A 98 through 5RP A 401
ChainResidue
AASP41
AMET60
APRO66
AMET78
AALA97
AALA99
ALEU110
AASP119
ASER121
AVAL123
ALEU124
AARG164
AALA169
AGLY170
AALA229
AGLY230
AGLY231
APHE250
AVAL251
AGLY252
ASER253
AHOH504
AHOH511
AHOH513
AHOH515
AHOH531
AHOH553

site_idAC6
Number of Residues28
Detailsbinding site for Poly-Saccharide residues LYS B 98 through 5RP B 401
ChainResidue
BASP41
BMET60
BLEU62
BPRO66
BMET78
BALA97
BALA99
BLEU110
BASP119
BSER121
BVAL123
BLEU124
BARG164
BALA169
BGLY170
BALA229
BGLY230
BGLY231
BPHE250
BVAL251
BGLY252
BSER253
BHOH504
BHOH511
BHOH512
BHOH518
BHOH525
BHOH532

site_idAC7
Number of Residues26
Detailsbinding site for Poly-Saccharide residues LYS C 98 through 5RP C 401
ChainResidue
CGLY231
CVAL251
CGLY252
CSER253
CHOH504
CHOH508
CHOH512
CHOH516
CHOH520
CHOH534
CASP41
CMET60
CPRO66
CMET78
CALA97
CALA99
CLEU110
CASP119
CSER121
CVAL123
CLEU124
CARG164
CALA169
CGLY170
CALA229
CGLY230

site_idAC8
Number of Residues28
Detailsbinding site for Poly-Saccharide residues LYS D 98 through 5RP D 401
ChainResidue
DASP41
DMET60
DLEU62
DPRO66
DMET78
DALA97
DALA99
DLEU110
DASP119
DSER121
DVAL123
DLEU124
DARG164
DALA169
DGLY170
DALA229
DGLY230
DGLY231
DPHE250
DVAL251
DGLY252
DSER253
DHOH513
DHOH515
DHOH518
DHOH519
DHOH529
DHOH573

Functional Information from PROSITE/UniProt
site_idPS01235
Number of Residues19
DetailsPDXS_SNZ_1 PdxS/SNZ family signature. LPVVQFAAGGVATPADAAL
ChainResidueDetails
ALEU222-LEU240

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Schiff-base intermediate with D-ribose 5-phosphate => ECO:0000250|UniProtKB:O59080
ChainResidueDetails
ALYS98
BLYS98
CLYS98
DLYS98

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O59080
ChainResidueDetails
AASP41
CGLY170
CGLY231
CGLY252
DASP41
DGLY170
DGLY231
DGLY252
AGLY170
AGLY231
AGLY252
BASP41
BGLY170
BGLY231
BGLY252
CASP41

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q03148
ChainResidueDetails
AARG182
BARG182
CARG182
DARG182

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET2
BMET2
CMET2
DMET2

222624

PDB entries from 2024-07-17

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