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3WQQ

Crystal structure of PfDXR complexed with inhibitor-3

Functional Information from GO Data
ChainGOidnamespacecontents
A0008299biological_processisoprenoid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0019288biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
A0020011cellular_componentapicoplast
A0030604molecular_function1-deoxy-D-xylulose-5-phosphate reductoisomerase activity
A0046872molecular_functionmetal ion binding
A0070402molecular_functionNADPH binding
B0008299biological_processisoprenoid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0019288biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
B0020011cellular_componentapicoplast
B0030604molecular_function1-deoxy-D-xylulose-5-phosphate reductoisomerase activity
B0046872molecular_functionmetal ion binding
B0070402molecular_functionNADPH binding
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NDP A 501
ChainResidue
AGLY84
ASER117
AHIS136
AGLY180
AILE181
AASP182
AGLN185
AALA203
AASN204
ALYS205
AGLU206
ATHR86
AASP231
AMET298
AGLY299
AMET360
AIB3503
AHOH615
AHOH628
AHOH653
AHOH670
AHOH684
AGLY87
ASER88
AILE89
ATYR113
AVAL114
AASN115
ALYS116

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
ALYS205
AASP231
AGLU233
AGLU315
AIB3503

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE IB3 A 503
ChainResidue
ALYS205
AASP231
ASER232
AGLU233
ASER269
ASER270
ATRP296
AMET298
AILE302
ASER306
AASN311
ALYS312
AGLU315
APRO358
ANDP501
AMG502
AHOH609
AHOH631

site_idAC4
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NDP B 501
ChainResidue
BGLY84
BTHR86
BGLY87
BSER88
BILE89
BTYR113
BVAL114
BASN115
BLYS116
BSER117
BHIS136
BGLY180
BILE181
BASP182
BGLN185
BALA203
BASN204
BLYS205
BGLU206
BASP231
BTRP296
BGLY299
BILE302
BMET360
BIB3505
BHOH604
BHOH665
BHOH685

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BLYS205
BASP231
BGLU233
BGLU315
BIB3505

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 503
ChainResidue
AASP242
AHOH614
BGLN239
BLEU241
BHOH633
BHOH637
BHOH656

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA B 504
ChainResidue
BASN452

site_idAC8
Number of Residues19
DetailsBINDING SITE FOR RESIDUE IB3 B 505
ChainResidue
BLYS295
BTRP296
BMET298
BSER306
BASN311
BLYS312
BGLU315
BCYS338
BPRO358
BNDP501
BMG502
BHOH608
BHOH621
BLYS205
BASP231
BSER232
BGLU233
BSER269
BSER270

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22355528, ECO:0007744|PDB:3AU8, ECO:0007744|PDB:3AU9, ECO:0007744|PDB:3AUA
ChainResidueDetails
ATHR86
AASN115
BTHR86
BASN115

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P45568
ChainResidueDetails
ALYS205
BSER270
BHIS293
BSER306
BASN311
BLYS312
ASER232
ASER270
AHIS293
ASER306
AASN311
ALYS312
BLYS205
BSER232

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22355528, ECO:0007744|PDB:3AU9, ECO:0007744|PDB:3AUA
ChainResidueDetails
AGLU206
AGLY299
BGLU206
BGLY299

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22355528, ECO:0007744|PDB:3AU8
ChainResidueDetails
AASP231
AGLU233
AGLU315
BASP231
BGLU233
BGLU315

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PDB entries from 2024-07-24

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