eF-site ID 2iik-AB
PDB Code 2iik
Chain A, B

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Title Crystal Structure of human peroxisomal acetyl-CoA acyl transferase 1 (ACAA1)
Classification TRANSFERASE
Compound 3-ketoacyl-CoA thiolase, peroxisomal
Source Homo sapiens (Human) (THIK_HUMAN)
Sequence A:  ASAADVVVVHGRRTAICRAGRGGFKDTTPDELLSAVMTAV
LKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPE
TVPLSTVNRQCSSGLQAVASIAGGIRNGSYDIGMACGVES
MSLADGNITSRLMEKEKARDCLIPMGITSENVAERFGISR
EKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGT
KRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSS
QVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDI
MGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCV
EKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKR
RGKRAYGVVSMCIGTGMGAAAVFEYP
B:  TENLYFQSMAPQASAADVVVVHGRRTAICRAGRGGFKDTT
PDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIM
ARIAQFLSDIPETVPLSTVNRQCSSGLQAVASIAGGIRNG
SYDIGMACGVESMSLAPGNITSRLMEKEKARDCLIPMGIT
SENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIV
PVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAF
KKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVL
RSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEI
NEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGA
RQVITLLNELKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN
Description


Functional site

1) chain A
residue 119-137
type prosite
sequence VNRQCSSGLQAVASIAGGI
description THIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNRqCSSGLqAVasiaggI
source prosite : PS00098

2) chain A
residue 404-417
type prosite
sequence GVVSMCIGTGMGAA
description THIOLASE_3 Thiolases active site. GVVSMCIGtGmGaA
source prosite : PS00099

3) chain A
residue 368-384
type prosite
sequence NPLGGAVALGHPLGCTG
description THIOLASE_2 Thiolases signature 2. NplGGaVAlGHPlGcTG
source prosite : PS00737

4) chain A
residue 123
type ACT_SITE
sequence C
description Acyl-thioester intermediate => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

5) chain B
residue 123
type ACT_SITE
sequence C
description Acyl-thioester intermediate => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

6) chain A
residue 378
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020
source Swiss-Prot : SWS_FT_FI2

7) chain A
residue 409
type ACT_SITE
sequence C
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020
source Swiss-Prot : SWS_FT_FI2

8) chain B
residue 378
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020
source Swiss-Prot : SWS_FT_FI2

9) chain B
residue 409
type ACT_SITE
sequence C
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020
source Swiss-Prot : SWS_FT_FI2

10) chain A
residue 59
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI3

11) chain A
residue 60
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI3

12) chain B
residue 59
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI3

13) chain B
residue 60
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI3


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