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5LBX

Structure of the T175V Etr1p mutant in the trigonal form P312 in complex with NADP and crotonyl-CoA

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 Residues20
Detailsbinding site for residue NAP A 401
ChainResidue
APRO69
AARG224
ATYR296
AGLY297
AMET299
APHE321
AVAL323
ALYS381
ACOO410
AHOH527
AHOH534
AVAL171
AHOH573
AASN172
AVAL175
ATHR199
ASER200
AALA201
AVAL202
AARG222

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 402
ChainResidue
ASER125
AHIS126
AVAL127
ALYS331

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 403
ChainResidue
ASER250
AARG251
AGLU252

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 A 404
ChainResidue
AVAL242
AGLN247

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 405
ChainResidue
ALYS145
AGLN151
AASN155

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 A 406
ChainResidue
AGLN33
AHIS34
ALYS85
AHOH544

site_idAC7
Number of Residues2
Detailsbinding site for residue SO4 A 407
ChainResidue
AARG224
AASN226

site_idAC8
Number of Residues2
Detailsbinding site for residue SO4 A 408
ChainResidue
BLYS278
BARG285

site_idAC9
Number of Residues2
Detailsbinding site for residue SO4 A 409
ChainResidue
AASN288
AASN289

site_idAD1
Number of Residues10
Detailsbinding site for residue COO A 410
ChainResidue
ASER70
AASN73
ATYR79
AGLY297
AGLY298
ATHR324
ANAP401
AHOH569
BTHR308
BSER309

site_idAD2
Number of Residues2
Detailsbinding site for residue CL A 411
ChainResidue
ALYS153
ALYS153

site_idAD3
Number of Residues20
Detailsbinding site for residue NAP B 401
ChainResidue
BVAL171
BASN172
BVAL175
BTHR199
BSER200
BALA201
BVAL202
BARG222
BARG224
BTYR296
BGLY297
BMET299
BPHE321
BVAL323
BLYS381
BCOO407
BHOH528
BHOH541
BHOH551
BHOH553

site_idAD4
Number of Residues3
Detailsbinding site for residue SO4 B 402
ChainResidue
BGLN33
BHIS34
BLYS85

site_idAD5
Number of Residues2
Detailsbinding site for residue SO4 B 403
ChainResidue
BVAL242
BGLN247

site_idAD6
Number of Residues3
Detailsbinding site for residue SO4 B 404
ChainResidue
BARG224
BASN226
BVAL230

site_idAD7
Number of Residues2
Detailsbinding site for residue SO4 B 405
ChainResidue
BARG222
BLYS378

site_idAD8
Number of Residues3
Detailsbinding site for residue SO4 B 406
ChainResidue
BASN288
BASN289
BHOH504

site_idAD9
Number of Residues11
Detailsbinding site for residue COO B 407
ChainResidue
ATHR308
ASER309
BSER70
BASN73
BTYR79
BGLY298
BMET299
BPHE301
BTHR324
BNAP401
BHOH503

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
AASN172
BTYR296
BPHE321
BLYS381
ATHR199
AARG222
ATYR296
APHE321
ALYS381
BASN172
BTHR199
BARG222

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

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PDB entries from 2024-07-24

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