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1PR9

Human L-Xylulose Reductase Holoenzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0004090molecular_functioncarbonyl reductase (NADPH) activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005881cellular_componentcytoplasmic microtubule
A0005886cellular_componentplasma membrane
A0005902cellular_componentmicrovillus
A0005903cellular_componentbrush border
A0005997biological_processxylulose metabolic process
A0006006biological_processglucose metabolic process
A0006739biological_processNADP metabolic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
A0019640biological_processglucuronate catabolic process to xylulose 5-phosphate
A0042732biological_processD-xylose metabolic process
A0042802molecular_functionidentical protein binding
A0050038molecular_functionL-xylulose reductase (NADPH) activity
A0070062cellular_componentextracellular exosome
A2000379biological_processpositive regulation of reactive oxygen species metabolic process
B0004090molecular_functioncarbonyl reductase (NADPH) activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005881cellular_componentcytoplasmic microtubule
B0005886cellular_componentplasma membrane
B0005902cellular_componentmicrovillus
B0005903cellular_componentbrush border
B0005997biological_processxylulose metabolic process
B0006006biological_processglucose metabolic process
B0006739biological_processNADP metabolic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
B0019640biological_processglucuronate catabolic process to xylulose 5-phosphate
B0042732biological_processD-xylose metabolic process
B0042802molecular_functionidentical protein binding
B0050038molecular_functionL-xylulose reductase (NADPH) activity
B0070062cellular_componentextracellular exosome
B2000379biological_processpositive regulation of reactive oxygen species metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE K A 246
ChainResidue
A2HP247

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 1246
ChainResidue
BTYR149
BHOH459
BHOH462
B2HP1247

site_idAC3
Number of Residues32
DetailsBINDING SITE FOR RESIDUE NAP A 245
ChainResidue
AILE19
ASER38
AARG39
ATHR40
AASP43
AVAL59
AASP60
ALEU61
AGLY62
AASN83
AALA85
AARG102
AVAL134
ASER135
ATYR149
ALYS153
APRO179
ATHR180
AVAL181
AVAL182
ATHR184
ASER185
AMET186
AHOH302
AHOH308
AHOH413
AHOH445
AHOH451
AGLY14
AGLY16
ALYS17
AGLY18

site_idAC4
Number of Residues35
DetailsBINDING SITE FOR RESIDUE NAP B 1245
ChainResidue
BGLY14
BGLY16
BLYS17
BGLY18
BILE19
BSER38
BARG39
BTHR40
BVAL59
BASP60
BLEU61
BGLY62
BASN83
BALA85
BVAL106
BVAL134
BSER135
BSER136
BTYR149
BLYS153
BPRO179
BTHR180
BVAL181
BVAL182
BTHR184
BSER185
BMET186
BGLY187
BHOH359
BHOH360
BHOH383
BHOH401
BHOH443
BHOH462
B2HP1247

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 2HP A 247
ChainResidue
ASER136
ACYS138
AHIS146
ATYR149
AVAL181
ATRP191
AK246

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 2HP B 1247
ChainResidue
BSER136
BCYS138
BVAL143
BHIS146
BVAL181
BMET200
BHOH459
BNAP1245
BK1246

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SqcsqravtnHsvYCSTKGALdMLTkVMA
ChainResidueDetails
ASER136-ALA164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR149
BTYR149

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15103634
ChainResidueDetails
ALEU11
ASER136
ALYS153
BLEU11
BSER136
BLYS153

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:12665801, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0007744|PubMed:24129315
ChainResidueDetails
AARG21
BARG21

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER46
BSER46

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ASER136
ATYR149
ALYS153

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BSER136
BTYR149
BLYS153

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ASER136
AASN107
ATYR149
ALYS153

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BSER136
BASN107
BTYR149
BLYS153

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
AHIS146
ALYS153

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BHIS146
BLYS153

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ATYR149
ALYS153

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BTYR149
BLYS153

224572

PDB entries from 2024-09-04

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