eF-site ID 3hmj-C
PDB Code 3hmj
Chain C

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Title Saccharomyces cerevisiae FAS type I
Classification TRANSFERASE
Compound Fatty acid synthase subunit alpha
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (FAS1_YEAST)
Sequence C:  MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFN
TERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILC
YSKDAKEIYYTPDPIADEPVKASLLLHVLVAHKLKKSLDS
IPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEETP
LEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTITV
ARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADAKA
FLDSMAQKYASIVGVDLLEEITKDHKVLARQQLQVLARYL
KMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFVNGV
ATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKNVDR
EVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQLVK
TLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGNIT
YSEEPREKVRKLSQYVQEMALGGPITKESQMDVEDALDKD
STKEVASLPNKSTISKTVSSTIPRETIPFLHLRKKTPAGD
WKYDRQLSSLFLDGLEKAAFNGVTFKDKYVLITGAGKGSI
GAEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGAK
GSTLIVVPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDAI
IPFAAIPEQGIELEHIDSKSEFAHRIMLTNILRMMGCVKK
QKSARGIETRPAQVILPMSPNHGTFGGDGMYSESKLSLET
LFNRWHSESWANQLTVCGAIIGWTRGTNNIIAEGIEKMGV
RTFSQKEMAFNLLGLLTPEVVELCQKSPVMADLNGGLQFV
PELKEFTAKLRKELVETSEVRKAVSIETALEHKVVNGNSA
DAAYAQVEIQPRANIQLDFPELKPYKQVKQIAPAELEGLL
DLERVIVVTGFAEVGPWGSARTRWEMEAFGEFSLEGCVEM
AWIMGFISYHNGNLKGRPYTGWVDSKTKEPVDDKDVKAKY
ETSILEHSGIRLIEPELFNGYNPEKKEMIQEVIVEEDLEP
FEASKETAEQFKHQHGDKVDIFEIPETGEYSVKLLKGATL
YIPKALRFDRLVAGQIPTGWNAKTYGISDDIISQVDPITL
FVLVSVVEAFIASGITDPYEMYKYVHVSEVGNCSGSGMGG
VSALRGMFKDRFKDEPVQNDILQESFINTMSAWVNMLLIS
SSGPIKTPVGACATSVESVDIGVETILSGKARICIVGGYD
DFQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSRPATTTR
NGFMEAQGAGIQIIMQADLALKMGVPIYGIVAMAATATDK
IGRSVPAPGKGILTTAREHHSSVKYASPNLNMKYRKRQLV
TREAQIKDWVENELEALKLEAEEIPSEDQNEFLLERTREI
HNEAESQLRAAQQQWGNDFYKRDPRIAPLRGALATYGLTI
DDLGVASFHGTSTKANDKNESATINEMMKHLGRSEGNPVI
GVFQKFLTGHPKGAAGAWMMNGALQILNSGIIPGNRNADN
VDKILEQFEYVLYPSKTLKTDGVRAVSITSFGFGQKGGQA
IVVHPDYLYGAITEDRYNEYVAKVSAREKSAYKFFHNGMI
YNKLFVSKEHAPYTDELEEDVYLDPLARVSKDKKSGSLTF
NSKNIQSKDSYINTIETAKMIENMTKEKVSNGVGVDVELI
TSINVENDTFIERNFTPQEIEYCSAQPSVQSSFAGTWSAK
EAVFKSLGVKSLGGGAALKDIEIVRVNKNAPAVELHGNAK
KAAEEAGVTDVKVSISHDDLQAVAVAVSTK
Description


Functional site

1) chain C
residue 1279
type
sequence F
description BINDING SITE FOR RESIDUE CER B 2748
source : AC2

2) chain C
residue 1304
type
sequence A
description BINDING SITE FOR RESIDUE CER C 2748
source : AC3

3) chain C
residue 1305
type
sequence C
description BINDING SITE FOR RESIDUE CER C 2748
source : AC3

4) chain C
residue 1343
type
sequence F
description BINDING SITE FOR RESIDUE CER C 2748
source : AC3

5) chain C
residue 1542
type
sequence H
description BINDING SITE FOR RESIDUE CER C 2748
source : AC3

6) chain C
residue 1583
type
sequence H
description BINDING SITE FOR RESIDUE CER C 2748
source : AC3

7) chain C
residue 1585
type
sequence K
description BINDING SITE FOR RESIDUE CER C 2748
source : AC3

8) chain C
residue 1644
type
sequence F
description BINDING SITE FOR RESIDUE CER C 2748
source : AC3

9) chain C
residue 1646
type
sequence F
description BINDING SITE FOR RESIDUE CER C 2748
source : AC3

10) chain C
residue 37
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI8

11) chain C
residue 958
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:17330950
source Swiss-Prot : SWS_FT_FI7

12) chain C
residue 1440
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:17330950
source Swiss-Prot : SWS_FT_FI7

13) chain C
residue 1305
type ACT_SITE
sequence C
description For acetyltransferase activity => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

14) chain C
residue 1542
type ACT_SITE
sequence H
description For acetyltransferase activity => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

15) chain C
residue 1583
type ACT_SITE
sequence H
description For acetyltransferase activity => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

16) chain C
residue 1772
type ACT_SITE
sequence D
description For malonyltransferase activity => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

17) chain C
residue 1773
type ACT_SITE
sequence V
description For malonyltransferase activity => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

18) chain C
residue 1774
type ACT_SITE
sequence E
description For malonyltransferase activity => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

19) chain C
residue 1817
type ACT_SITE
sequence E
description For malonyltransferase activity => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

20) chain C
residue 1841
type ACT_SITE
sequence R
description For malonyltransferase activity => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

21) chain C
residue 1871
type ACT_SITE
sequence I
description For malonyltransferase activity => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

22) chain C
residue 1872
type ACT_SITE
sequence S
description For malonyltransferase activity => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

23) chain C
residue 1873
type ACT_SITE
sequence H
description For malonyltransferase activity => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

24) chain C
residue 1798
type MOD_RES
sequence Y
description N-acetylmethionine => ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI3

25) chain C
residue 1808
type MOD_RES
sequence S
description N-acetylmethionine => ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI3


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