eF-site ID 6ql5-D
PDB Code 6ql5
Chain D

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Title Structure of fatty acid synthase complex with bound gamma subunit from Saccharomyces cerevisiae at 2.8 angstrom
Classification TRANSFERASE
Compound Fatty acid synthase subunit alpha
Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae;
Sequence D:  MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFN
TERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILC
YSKDAKEIYYTPDPIADEPVKASLLLHVLVAHKLKKSLDS
IPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEETP
LEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTITV
ARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADAKA
FLDSMAQKYASIVGVDLLEEITKDHKVLARQQLQVLARYL
KMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFVNGV
ATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKNVDR
EVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQLVK
TLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGNIT
YSEEPREKVRKLSQYVQEMALGGPITKESALDKDSTKEVA
SLPNKSTISKTVSSTIPRETIPFLHLRKKTPAGDWKYDRQ
LSSLFLDGLEKAAFNGVTFKDKYVLITGAGKGSIGAEVLQ
GLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGAKGSTLIV
VPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDAIIPFAAI
PEQGIELEHIDSKSEFAHRIMLTNILRMMGCVKKQKSARG
IETRPAQVILPMSPNHGTFGGDGMYSESKLSLETLFNRWH
SESWANQLTVCGAIIGWTRGTGLMSANNIIAEGIEKMGVR
TFSQKEMAFNLLGLLTPEVVELCQKSPVMADLNGGLQFVP
ELKEFTAKLRKELVETSEVRKAVSIETALEHKVVNGNSAD
AAYAQVEIQPRANIQLDFPELKPYKQVKQIAPAELEGLLD
LERVIVVTGFAEVGPWGSARTRWEMEAFGEFSLEGCVEMA
WIMGFISYHNGNLKGRPYTGWVDSKTKEPVDDKDVKAKYE
TSILEHSGIRLIEPELFNGYNPEKKEMIQEVIVEEDLEPF
EASKETAEQFKHQHGDKVDIFEIPETGEYSVKLLKGATLY
IPKALRFDRLVAGQIPTGWNAKTYGISDDIISQVDPITLF
VLVSVVEAFIASGITDPYEMYKYVHVSEVGNCSGSGMGGV
SALRGMFKDRFKDEPVQNDILQESFINTMSAWVNMLLISS
SGPIKTPVGACATSVESVDIGVETILSGKARICIVGGYDD
FQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSRPATTTRN
GFMEAQGAGIQIIMQADLALKMGVPIYGIVAMAATATDKI
GRSVPAPGKGILTTAREHHSSVKYASPNLNMKYRKRQLVT
REAQIKDWVENELEALKLEAEEIPSEDQNEFLLERTREIH
NEAESQLRAAQQQWGNDFYKRDPRIAPLRGALATYGLTID
DLGVASFHGTSTKANDKNESATINEMMKHLGRSEGNPVIG
VFQKFLTGHPKGAAGAWMMNGALQILNSGIIPGNRNADNV
DKILEQFEYVLYPSKTLKTDGVRAVSITSFGFGQKGGQAI
VVHPDYLYGAITEDRYNEYVAKVSAREKSAYKFFHNGMIY
NKLFVSKEHAPYTDELEEDVYLDPLARVSKDKKSGSLTFN
SKNIQSKDSYINANTIETAKMIENMTKEKVSNGGVGVDVE
LITSINVENDTFIERNFTPQEIEYCSAQPSVQSSFAGTWS
AKEAVFKSLGVKSLGGGAALKDIEIVRVNKNAPAVELHGN
AKKAAEEAGVTDVKVSISHDDLQAVAVAVSTK
Description (1)  Fatty acid synthase subunit alpha (E.C.2.3.1.86,1.1.1.100,2.3.1.41), Fatty acid synthase subunit beta (E.C.2.3.1.86,4.2.1.59,1.3.1.9,2.3.1.38,2.3.1.39,3.1.2.14), Translation machinery-associated protein 17


Functional site

1) chain D
residue 178
type
sequence G
description binding site for Di-peptide PNS D 1901 and SER D 180
source : AD1

2) chain D
residue 179
type
sequence K
description binding site for Di-peptide PNS D 1901 and SER D 180
source : AD1

3) chain D
residue 181
type
sequence T
description binding site for Di-peptide PNS D 1901 and SER D 180
source : AD1

4) chain D
residue 182
type
sequence V
description binding site for Di-peptide PNS D 1901 and SER D 180
source : AD1

5) chain D
residue 183
type
sequence Q
description binding site for Di-peptide PNS D 1901 and SER D 180
source : AD1

6) chain D
residue 184
type
sequence N
description binding site for Di-peptide PNS D 1901 and SER D 180
source : AD1

7) chain D
residue 1305
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI1

8) chain D
residue 1542
type MOD_RES
sequence H
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI1

9) chain D
residue 1583
type MOD_RES
sequence H
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI1

10) chain D
residue 1772
type MOD_RES
sequence D
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

11) chain D
residue 1773
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

12) chain D
residue 1774
type MOD_RES
sequence E
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

13) chain D
residue 1817
type MOD_RES
sequence E
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

14) chain D
residue 1841
type MOD_RES
sequence R
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

15) chain D
residue 1871
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

16) chain D
residue 1872
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

17) chain D
residue 1873
type MOD_RES
sequence H
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

18) chain D
residue 1798
type MOD_RES
sequence Y
description Phosphothreonine => ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI3

19) chain D
residue 1808
type MOD_RES
sequence S
description Phosphothreonine => ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI3

20) chain D
residue 180
type CROSSLNK
sequence S
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI5

21) chain D
residue 523
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI6

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

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

24) chain D
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


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