Structure of PDB 2vkz Chain A

Receptor sequence
>2vkzA (length=1614) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFNTERVVEIGPS
PTLAGMAQRTLKNKYESYDAALSLHREILCYSKDAKEIYYTPDPIADEPV
KASLLLHVLVAHKLKKSLDSIPMSKTIKDLVGGKSTVQNEILGDLGKEFG
TTPEKPEETPLEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTITV
ARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADAKAFLDSMAQKYA
SIVGVDLLEEITKDHKVLARQQLQVLARYLKMDLDNGERKFLKEKDTVAE
LQAQLDYLNAELGEFFVNGVATSFSRKKARTFDSSWNWAKQSLLSLYFEI
IHGVLKNVDREVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQLVK
TLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGNITYSEEPREKVR
KLSQYVQEMALGGPITKESQMDVEDALDKDSTKEVASLPNKSTISKTVSS
TIPRETIPFLHLRKKTPAGDWKYDRQLSSLFLDGLEKAAFNGVTFKDKYV
LITGAGKGSIGAEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGAK
GSTLIVVPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDAIIPFAAIPEQG
IELEHIDSKSEFAHRIMLTNILRMMGCVKKQKSARGIETRPAQVILPMSP
NHGTFGGDGMYSESKLSLETLFNRWHSESWANQLTVCGAIIGWTRGTNNI
IAEGIEKMGVRTFSQKEMAFNLLGLLTPEVVELCQKSPVMADLNGGLQFV
PELKEFTAKLRKELVETSEVRKAVSIETALEHKVVNGNSADAAYAQVEIQ
PRANIQLDFPELKPYKQVKQIAPAELEGLLDLERVIVVTGFAEVGPWGSA
RTRWEMEAFGEFSLEGCVEMAWIMGFISYHNGNLKGRPYTGWVDSKTKEP
VDDKDVKAKYETSILEHSGIRLIEPELFNGYNPEKKEMIQEVIVEEDLEP
FEASKETAEQFKHQHGDKVDIFEIPETGEYSVKLLKGATLYIPKALRFDR
LVAGQIPTGWNAKTYGISDDIISQVDPITLFVLVSVVEAFIASGITDPYE
MYKYVHVSEVGNCSGSGMGGVSALRGMFKDRFKDEPVQNDILQESFINTM
SAWVNMLLISSSGPIKTPVGACATSVESVDIGVETILSGKARICIVGGYD
DFQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSRPATTTRNGFMEAQGAG
IQIIMQADLALKMGVPIYGIVAMAATATDKIGRSVPAPGKGILTTAREHH
SSVKYASPNLNMKYRKRQLVTREAQIKDWVENELEALKLEAEEIPSEDQN
EFLLERTREIHNEAESQLRAAQQQWGNDFYKRDPRIAPLRGALATYGLTI
DDLGVASFHGTSTKANDKNESATINEMMKHLGRSEGNPVIGVFQKFLTGH
PKGAAGAWMMNGALQILNSGIIPGNRNADNVDKILEQFEYVLYPSKTLKT
DGVRAVSITSFGFGQKGGQAIVVHPDYLYGAITEDRYNEYVAKVSAREKS
AYKFFHNGMIYNKLFVSKEHAPYTDELEEDVYLDPLARVSKDKKSGSLTF
NSKNIQSKDSYINA
3D structure
PDB2vkz Inhibition of the Fungal Fatty Acid Synthase Type I Multienzyme Complex.
ChainA
Resolution4.0 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) C1172 H1409 E1420 K1445 H1450 F1511 F1513
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 CER A A1304 C1305 F1343 H1583 K1585 F1646 A1171 C1172 F1210 H1450 K1452 F1513
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
View graph for
Cellular Component
External links
PDB RCSB:2vkz, PDBe:2vkz, PDBj:2vkz
PDBsum2vkz
PubMed18725634
UniProtP19097|FAS2_YEAST Fatty acid synthase subunit alpha (Gene Name=FAS2)

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