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5LB9

Structure of the T175V Etr1p mutant in the monoclinic form P21

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0019166molecular_functiontrans-2-enoyl-CoA reductase (NADPH) activity
A0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
B0005739cellular_componentmitochondrion
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0019166molecular_functiontrans-2-enoyl-CoA reductase (NADPH) activity
B0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue GOL A 401
ChainResidue
ALYS204
AALA353
AHOH515

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 402
ChainResidue
AARG251
AARG285
ASER309
ANA412

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 403
ChainResidue
AHOH501
AHOH544
ALYS278
AARG285

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 404
ChainResidue
AGLN151
AHOH512
AHOH546
AHOH620
BLYS61
BHOH557

site_idAC5
Number of Residues17
Detailsbinding site for residue NAP A 405
ChainResidue
AVAL171
AASN172
ATHR199
ASER200
AALA201
AVAL202
AARG222
AARG224
ATYR296
AMET299
APHE321
ATRP322
AVAL323
ALYS381
ASO4406
AHOH573
AHOH621

site_idAC6
Number of Residues8
Detailsbinding site for residue SO4 A 406
ChainResidue
AGLY197
AGLY198
ATHR199
AILE221
AARG222
AARG224
ANAP405
AHOH526

site_idAC7
Number of Residues7
Detailsbinding site for residue SO4 A 407
ChainResidue
AASN100
APRO124
AHIS126
AVAL127
ASER170
ALYS334
AGOL414

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 A 408
ChainResidue
AHIS126
AVAL127
ALYS331
AGOL414

site_idAC9
Number of Residues6
Detailsbinding site for residue SO4 A 409
ChainResidue
AASN248
ASER250
AARG251
AARG285
ALYS286
AHOH510

site_idAD1
Number of Residues3
Detailsbinding site for residue SO4 A 410
ChainResidue
AASN288
AASN289
ALYS314

site_idAD2
Number of Residues2
Detailsbinding site for residue SO4 A 411
ChainResidue
AGLN33
AHIS34

site_idAD3
Number of Residues4
Detailsbinding site for residue NA A 412
ChainResidue
ATHR308
ASER309
ASO4402
AHOH631

site_idAD4
Number of Residues9
Detailsbinding site for residue GOL A 413
ChainResidue
ATYR311
AILE312
AASN315
AHOH536
AHOH558
BGLY320
BTRP322
BGLU325
BHOH521

site_idAD5
Number of Residues6
Detailsbinding site for residue GOL A 414
ChainResidue
AVAL127
ASER170
ATHR324
ALYS334
ASO4407
ASO4408

site_idAD6
Number of Residues9
Detailsbinding site for residue GOL B 401
ChainResidue
AGLY320
APHE321
ATRP322
AHOH511
BTYR311
BILE312
BASN315
BHOH512
BHOH571

site_idAD7
Number of Residues3
Detailsbinding site for residue GOL B 402
ChainResidue
BTHR91
BTHR92
BGLU93

site_idAD8
Number of Residues10
Detailsbinding site for residue SO4 B 403
ChainResidue
BARG222
BARG224
BHOH510
BHOH641
BHOH672
BHOH695
BGLY197
BGLY198
BTHR199
BILE221

site_idAD9
Number of Residues4
Detailsbinding site for residue SO4 B 404
ChainResidue
BGLN33
BHIS34
BHOH559
BHOH637

site_idAE1
Number of Residues3
Detailsbinding site for residue SO4 B 405
ChainResidue
BARG285
BSER309
BNA408

site_idAE2
Number of Residues9
Detailsbinding site for residue SO4 B 406
ChainResidue
BPRO69
BASN172
BALA201
BLYS381
BNA407
BHOH611
BHOH614
BHOH678
BHOH700

site_idAE3
Number of Residues2
Detailsbinding site for residue NA B 407
ChainResidue
BALA201
BSO4406

site_idAE4
Number of Residues4
Detailsbinding site for residue NA B 408
ChainResidue
BTHR308
BSER309
BSO4405
BHOH662

site_idAE5
Number of Residues3
Detailsbinding site for residue GOL B 409
ChainResidue
BHIS182
BHOH521
BHOH570

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:25867044
ChainResidueDetails
ATYR79
BTYR79

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:12614607, ECO:0000269|PubMed:12890667
ChainResidueDetails
AARG222
ATYR296
APHE321
ALYS381
BASN172
BTHR199
BARG222
BTYR296
BPHE321
BLYS381
AASN172
ATHR199

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 620
ChainResidueDetails
ATYR79electrostatic stabiliser, increase electrophilicity

site_idMCSA2
Number of Residues1
DetailsM-CSA 620
ChainResidueDetails
BTYR79electrostatic stabiliser, increase electrophilicity

220472

PDB entries from 2024-05-29

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