eF-site ID 1afw-AB
PDB Code 1afw
Chain A, B

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Title THE 1.8 ANGSTROM CRYSTAL STRUCTURE OF THE DIMERIC PEROXISOMAL THIOLASE OF SACCHAROMYCES CEREVISIAE
Classification THIOLASE
Compound 3-KETOACETYL-COA THIOLASE
Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae;
Sequence A:  KNSLLEKRPEDVVIVAANRSAIGKGFKGAFKDVNTDYLLY
NFLNEFIGRFPEPLRADLNLIEEVACGNVLNVGAGATEHR
AACLASGIPYSTPFVALNRQCSSGLTAVNDIANKIKVGQI
DIGLALGVESMTNNYKNVNPLGMISSEELQKNREAKKCLI
PMGITNENVAANFKISRKDQDEFAANSYQKAYKAKNEGLF
EDEILPIKLPDGSICQSDEGPRPNVTAESLSSIRPAFIGT
TTAGNASQVSDGVAGVLLARRSVANQLNLPVLGRYIDFQT
VGVPPEIMGVGPAYAIPKVLEATGLQVQDIDIFEINEAFA
AQALYCIHKLGIDLNKVNPRGGAIALGHPLGCTGARQVAT
ILRELKKDQIGVVSMCIGTGMGAAAIFIKE
B:  KNSLLEKRPEDVVIVAANRSAIGKGFKGAFKDVNTDYLLY
NFLNEFIGRFPEPLRADLNLIEEVACGNVLNVGAGATEHR
AACLASGIPYSTPFVALNRQCSSGLTAVNDIANKIKVGQI
DIGLALGVESMTNNYKNVNPLGMISSEELQKNREAKKCLI
PMGITNENVAANFKISRKDQDEFAANSYQKAYKAKNEGLF
EDEILPIKLPDGSICQSDEGPRPNVTAESLSSIRPAFIKD
RGTTTAGNASQVSDGVAGVLLARRSVANQLNLPVLGRYID
FQTVGVPPEIMGVGPAYAIPKVLEATGLQVQDIDIFEINE
AFAAQALYCIHKLGIDLNKVNPRGGAIALGHPLGCTGARQ
VATILRELKKDQIGVVSMCIGTGMGAAAIFIKE
Description


Functional site

1) chain A
residue 125
type
sequence C
description ACTIVE SITE IN CHAIN A.
source : AVA

2) chain A
residue 375
type
sequence H
description ACTIVE SITE IN CHAIN A.
source : AVA

3) chain A
residue 403
type
sequence C
description ACTIVE SITE IN CHAIN A.
source : AVA

4) chain B
residue 125
type
sequence C
description ACTIVE SITE IN CHAIN B.
source : AVB

5) chain B
residue 375
type
sequence H
description ACTIVE SITE IN CHAIN B.
source : AVB

6) chain B
residue 403
type
sequence C
description ACTIVE SITE IN CHAIN B.
source : AVB

7) chain A
residue 124
type
sequence Q
description BINDING SITE FOR RESIDUE MRD A 501
source : AC1

8) chain A
residue 182
type
sequence C
description BINDING SITE FOR RESIDUE MRD A 501
source : AC1

9) chain A
residue 183
type
sequence L
description BINDING SITE FOR RESIDUE MRD A 501
source : AC1

10) chain A
residue 184
type
sequence I
description BINDING SITE FOR RESIDUE MRD A 501
source : AC1

11) chain B
residue 124
type
sequence Q
description BINDING SITE FOR RESIDUE MRD B 502
source : AC2

12) chain B
residue 182
type
sequence C
description BINDING SITE FOR RESIDUE MRD B 502
source : AC2

13) chain B
residue 183
type
sequence L
description BINDING SITE FOR RESIDUE MRD B 502
source : AC2

14) chain B
residue 184
type
sequence I
description BINDING SITE FOR RESIDUE MRD B 502
source : AC2

15) chain A
residue 125
type ACT_SITE
sequence C
description Acyl-thioester intermediate
source Swiss-Prot : SWS_FT_FI1

16) chain B
residue 125
type ACT_SITE
sequence C
description Acyl-thioester intermediate
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 125
type catalytic
sequence C
description 77
source MCSA : MCSA1

18) chain A
residue 375
type catalytic
sequence H
description 77
source MCSA : MCSA1

19) chain A
residue 403
type catalytic
sequence C
description 77
source MCSA : MCSA1

20) chain A
residue 405
type catalytic
sequence G
description 77
source MCSA : MCSA1

21) chain B
residue 125
type catalytic
sequence C
description 77
source MCSA : MCSA2

22) chain B
residue 375
type catalytic
sequence H
description 77
source MCSA : MCSA2

23) chain B
residue 403
type catalytic
sequence C
description 77
source MCSA : MCSA2

24) chain B
residue 405
type catalytic
sequence G
description 77
source MCSA : MCSA2

25) chain A
residue 375
type ACT_SITE
sequence H
description Proton acceptor
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 403
type ACT_SITE
sequence C
description Proton acceptor
source Swiss-Prot : SWS_FT_FI2

27) chain B
residue 375
type ACT_SITE
sequence H
description Proton acceptor
source Swiss-Prot : SWS_FT_FI2

28) chain B
residue 403
type ACT_SITE
sequence C
description Proton acceptor
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 121-139
type prosite
sequence LNRQCSSGLTAVNDIANKI
description THIOLASE_1 Thiolases acyl-enzyme intermediate signature. LNRqCSSGLtAVndiankI
source prosite : PS00098

30) chain A
residue 398-411
type prosite
sequence GVVSMCIGTGMGAA
description THIOLASE_3 Thiolases active site. GVVSMCIGtGmGaA
source prosite : PS00099

31) chain A
residue 365-381
type prosite
sequence NPRGGAIALGHPLGCTG
description THIOLASE_2 Thiolases signature 2. NprGGaIAlGHPlGcTG
source prosite : PS00737


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