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

click to enlarge
Title The Crystal Structure of the one-iron form of the di-iron center in 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 105
type
sequence E
description BINDING SITE FOR RESIDUE FE2 E 364
source : AC5

2) chain E
residue 143
type
sequence E
description BINDING SITE FOR RESIDUE FE2 E 364
source : AC5

3) chain E
residue 146
type
sequence H
description BINDING SITE FOR RESIDUE FE2 E 364
source : AC5

4) chain E
residue 229
type
sequence E
description BINDING SITE FOR RESIDUE FE2 E 364
source : AC5

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

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

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

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

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

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

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

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

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

14) 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

15) 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

16) 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

17) 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

18) 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

19) 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


Display surface

Download
Links