eF-site ID 1oq7-E
PDB Code 1oq7
Chain E

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Title The crystal structure of the iron free (Apo-)form of Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean).
Classification OXIDOREDUCTASE
Compound Acyl-[acyl-carrier protein] desaturase
Source Ricinus communis (Castor bean) (STAD_RICCO)
Sequence E:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP
VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV
LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR
AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM
DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK
LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD
MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY
ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL
EERAQGRAKEAPTMPFSWIFDRQVKL
Description


Functional site

1) chain E
residue 106
type
sequence E
description BINDING SITE FOR RESIDUE SR E 364
source : AC3

2) chain E
residue 148
type
sequence D
description BINDING SITE FOR RESIDUE SR E 364
source : AC3

3) chain E
residue 77
type
sequence D
description BINDING SITE FOR RESIDUE SR F 364
source : AC6

4) chain E
residue 62
type catalytic
sequence W
description 136
source MCSA : MCSA5

5) chain E
residue 105
type catalytic
sequence E
description 136
source MCSA : MCSA5

6) chain E
residue 143
type catalytic
sequence E
description 136
source MCSA : MCSA5

7) chain E
residue 146
type catalytic
sequence H
description 136
source MCSA : MCSA5

8) chain E
residue 196
type catalytic
sequence E
description 136
source MCSA : MCSA5

9) chain E
residue 199
type catalytic
sequence T
description 136
source MCSA : MCSA5

10) chain E
residue 228
type catalytic
sequence D
description 136
source MCSA : MCSA5

11) chain E
residue 229
type catalytic
sequence E
description 136
source MCSA : MCSA5

12) chain E
residue 232
type catalytic
sequence H
description 136
source MCSA : MCSA5

13) chain E
residue 105
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

14) chain E
residue 143
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

15) chain E
residue 146
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

16) chain E
residue 196
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

17) chain E
residue 229
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

18) chain E
residue 232
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1


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