eF-site ID 4o9c-C
PDB Code 4o9c
Chain C

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Title Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16
Classification TRANSFERASE
Compound Acetyl-CoA acetyltransferase
Source Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) (THIL_CUPNH)
Sequence C:  MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALER
AGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVP
AMTINKVSGSGLKAVMLAANAIMAGDAEIVVAGGQENMSA
APHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGIT
AENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIV
PVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAG
TVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYA
NAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAF
AAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILV
TLLHEMKRRDAKKGLASLCIGGGMGVALAVERK
Description


Functional site

1) chain C
residue 88
type
sequence S
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

2) chain C
residue 148
type
sequence L
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

3) chain C
residue 156
type
sequence H
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

4) chain C
residue 221
type
sequence R
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

5) chain C
residue 236
type
sequence F
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

6) chain C
residue 244
type
sequence A
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

7) chain C
residue 248
type
sequence S
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

8) chain C
residue 249
type
sequence G
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

9) chain C
residue 250
type
sequence L
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

10) chain C
residue 319
type
sequence A
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

11) chain C
residue 320
type
sequence F
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

12) chain C
residue 349
type
sequence H
description BINDING SITE FOR RESIDUE COA C 401
source : AC1

13) chain C
residue 88
type ACT_SITE
sequence S
description Acyl-thioester intermediate => ECO:0000269|PubMed:25152395
source Swiss-Prot : SWS_FT_FI1

14) chain C
residue 349
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395
source Swiss-Prot : SWS_FT_FI2

15) chain C
residue 379
type ACT_SITE
sequence C
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395
source Swiss-Prot : SWS_FT_FI2


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