Structure of PDB 6ql9 Chain E

Receptor sequence
>6ql9E (length=1759) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFNTERVVEIGPS
PTLAGMAQRTLKNKYESYDAALSLHREILCYSKDAKEIYYTPDPSEIADE
PVKASLLLHVLVAHKLKKSLDSIPMSKTIKDLVGGKSTVQNEILGDLGKE
FGTTPEKPEETPLEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTI
TVARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADAKAFLDSMAQK
YASIVGVDLLEEITKDHKVLARQQLQVLARYLKMDLDNGERKFLKEKDTV
AELQAQLDYLNAELGEFFVNGVATSFSRKKARTFDSSWNWAKQSLLSLYF
EIIHGVLKNVDREVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQL
VKTLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGNITYSEEPREK
VRKLSQYVQEMALGGPITKESMDVEDALDKDSTKEVASLPNKSTISKTVS
STIPRETIPFLHLRKKTPAGDWKYDRQLSSLFLDGLEKAAFNGVTFKDKY
VLITGAGKGSIGAEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGA
KGSTLIVVPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDAIIPFAAIPEQ
GIELEHIDSKSEFAHRIMLTNILRMMGCVKKQKSARGIETRPAQVILPMS
PNHGTFGGDGMYSESKLSLETLFNRWHSESWANQLTVCGAIIGWTRGTGL
MSANNIIAEGIEKMGVRTFSQKEMAFNLLGLLTPEVVELCQKSPVMADLN
GGLQFVPELKEFTAKLRKELVETSEVRKAVSIETALEHKVVNGNSADAAY
AQVEIQPRANIQLDFPELKPYKQVKQIAPAELEGLLDLERVIVVTGFAEV
GPWGSARTRWEMEAFGEFSLEGCVEMAWIMGFISYHNGNLKGRPYTGWVD
SKTKEPVDDKDVKAKYETSILEHSGIRLIEPELFNGYNPEKKEMIQEVIV
EEDLEPFEASKETAEQFKHQHGDKVDIFEIPETGEYSVKLLKGATLYIPK
ALRFDRLVAGQIPTGWNAKTYGISDDIISQVDPITLFVLVSVVEAFIASG
ITDPYEMYKYVHVSEVGNCSGSGMGGVSALRGMFKDRFKDEPVQNDILQE
SFINTMSAWVNMLLISSSGPIKTPVGACATSVESVDIGVETILSGKARIC
IVGGYDDFQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSRPATTTRNGFM
EAQGAGIQIIMQADLALKMGVPIYGIVAMAATATDKIGRSVPAPGKGILT
TAREHHSSVKYASPNLNMKYRKRQLVTREAQIKDWVENELEALKLEAEEI
PSEDQNEFLLERTREIHNEAESQLRAAQQQWGNDFYKRDPRIAPLRGALA
TYGLTIDDLGVASFHGTSTKANDKNESATINEMMKHLGRSEGNPVIGVFQ
KFLTGHPKGAAGAWMMNGALQILNSGIIPGNRNADNVDKILEQFEYVLYP
SKTLKTDGVRAVSITSFGFGQKGGQAIVVHPDYLYGAITEDRYNEYVAKV
SAREKSAYKFFHNGMIYNKLFVSKEHAPYTDELEEDVYLDPLARVSKDKK
SGSLTFNSKNIQSKDSYINANTIETAKMIENMTKEKVSNGGVGVDVELIT
SINVENDTFIERNFTPQEIEYCSAQPSVQSSFAGTWSAKEAVFKSLGVKS
LGGGAALKDIEIVRVNKNAPAVELHGNAKKAAEEAGVTDVKVSISHDDLQ
AVAVAVSTK
3D structure
PDB6ql9 Discovery of a Regulatory Subunit of the Yeast Fatty Acid Synthase.
ChainE
Resolution2.82 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C1305 H1542 E1553 K1578 H1583 F1644 F1646
Catalytic site (residue number reindexed from 1) C1178 H1415 E1426 K1451 H1456 F1517 F1519
Enzyme Commision number 1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase.
2.3.1.41: beta-ketoacyl-[acyl-carrier-protein] synthase I.
2.3.1.86: fatty-acyl-CoA synthase system.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PNS E C1305 F1376 S1417 P1419 A1420 H1542 T1544 T1546 N1549 F1644 C1178 F1249 S1290 P1292 A1293 H1415 T1417 T1419 N1422 F1517
BS02 A2P E G682 S708 A772 A773 G555 S581 A645 A646
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004312 fatty acid synthase activity
GO:0004315 3-oxoacyl-[acyl-carrier-protein] synthase activity
GO:0004316 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
GO:0004321 fatty-acyl-CoA synthase activity
GO:0005515 protein binding
GO:0008897 holo-[acyl-carrier-protein] synthase activity
GO:0016491 oxidoreductase activity
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0042759 long-chain fatty acid biosynthetic process
Cellular Component
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005835 fatty acid synthase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6ql9, PDBe:6ql9, PDBj:6ql9
PDBsum6ql9
PubMed32160528
UniProtP19097|FAS2_YEAST Fatty acid synthase subunit alpha (Gene Name=FAS2)

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