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5LNU

Crystal structure of Arabidopsis thaliana Pdx1-I320 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 Residues13
Detailsbinding site for residue PO4 A 401
ChainResidue
APRO66
AHOH505
AHOH508
AHOH543
AHOH619
ALYS166
AGLU168
AGLY170
AGLY230
AGLY231
AGLY252
ASER253
AKIK403

site_idAC2
Number of Residues10
Detailsbinding site for residue SO4 A 402
ChainResidue
AHIS132
AGLU151
AARG154
AARG155
AHOH533
AHOH544
AHOH583
AHOH586
AHOH613
DLYS204

site_idAC3
Number of Residues7
Detailsbinding site for residue KIK A 403
ChainResidue
AASP41
ALYS98
ASER121
AVAL123
AARG164
ALYS166
APO4401

site_idAC4
Number of Residues13
Detailsbinding site for residue PO4 B 401
ChainResidue
BPRO66
BLYS166
BGLU168
BGLY170
BGLY230
BGLY231
BGLY252
BSER253
BKIK403
BHOH506
BHOH508
BHOH545
BHOH623

site_idAC5
Number of Residues8
Detailsbinding site for residue SO4 B 402
ChainResidue
BHIS132
BGLU151
BARG154
BARG155
BHOH551
BHOH636
CLYS204
CHOH634

site_idAC6
Number of Residues14
Detailsbinding site for residue PO4 C 401
ChainResidue
CPRO66
CLYS166
CGLU168
CALA169
CGLY170
CGLY230
CGLY231
CGLY252
CSER253
CKIK403
CHOH501
CHOH502
CHOH558
CHOH635

site_idAC7
Number of Residues11
Detailsbinding site for residue SO4 C 402
ChainResidue
BLYS204
CHIS132
CGLU151
CARG154
CARG155
CHOH507
CHOH528
CHOH602
CHOH604
CHOH613
CHOH668

site_idAC8
Number of Residues14
Detailsbinding site for residue PO4 D 401
ChainResidue
DPRO66
DLYS166
DGLU168
DALA169
DGLY170
DGLY230
DGLY231
DGLY252
DSER253
DKIK403
DHOH509
DHOH514
DHOH584
DHOH599

site_idAC9
Number of Residues9
Detailsbinding site for residue SO4 D 402
ChainResidue
ALYS204
DHIS132
DGLU151
DARG154
DARG155
DHOH547
DHOH565
DHOH593
DHOH628

site_idAD1
Number of Residues15
Detailsbinding site for Di-peptide KIK B 403 and LYS B 98
ChainResidue
BASP41
BMET60
BALA61
BMET78
BALA97
BALA99
BLEU110
BASP119
BSER121
BVAL123
BLEU124
BARG164
BLYS166
BPO4401
BHOH531

site_idAD2
Number of Residues13
Detailsbinding site for Di-peptide KIK B 403 and LYS B 166
ChainResidue
BASP41
BLYS98
BSER121
BGLU122
BVAL123
BCYS146
BARG164
BTHR165
BGLY167
BALA169
BHIS180
BALA229
BPO4401

site_idAD3
Number of Residues13
Detailsbinding site for Di-peptide KIK C 403 and LYS C 166
ChainResidue
CASP41
CLYS98
CSER121
CGLU122
CVAL123
CCYS146
CARG164
CTHR165
CGLY167
CHIS180
CALA229
CGLY230
CPO4401

site_idAD4
Number of Residues14
Detailsbinding site for Di-peptide KIK C 403 and LYS C 98
ChainResidue
CASP41
CMET60
CALA61
CALA97
CALA99
CLEU110
CASP119
CSER121
CVAL123
CLEU124
CARG164
CLYS166
CPO4401
CHOH569

site_idAD5
Number of Residues13
Detailsbinding site for Di-peptide KIK D 403 and LYS D 166
ChainResidue
DASP41
DLYS98
DSER121
DGLU122
DVAL123
DCYS146
DARG164
DTHR165
DGLY167
DALA169
DHIS180
DALA229
DPO4401

site_idAD6
Number of Residues14
Detailsbinding site for Di-peptide KIK D 403 and LYS D 98
ChainResidue
DASP41
DMET60
DALA61
DALA97
DALA99
DLEU110
DASP119
DSER121
DVAL123
DLEU124
DARG164
DLYS166
DPO4401
DHOH578

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

224931

PDB entries from 2024-09-11

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