eF-site ID 1svd-AM
PDB Code 1svd
Chain A, M

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Title The structure of Halothiobacillus neapolitanus RuBisCo
Classification LYASE
Compound ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
Source ORGANISM_SCIENTIFIC: Halothiobacillus neapolitanus;
Sequence A:  TYWMPEYTPLDSDILACFKITPQPGVDREEAAAAVAAESS
TGTWTTVWTDLLTDMDYYKGRAYRIEDVPGDDAAFYAFIA
YPIDLFEEGSVVNVFTSLVGNVFGFKAVRGLRLEDVRFPL
AYVKTCGGPPHGIQVERDKMNKYGRPLLGCTIKPKLGLSA
KNYGRAVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVQ
DATETAEAQTGERKGHYLNVTAPTPEEMYKRAEFAKEIGA
PIIMHDYITGGFTANTGLAKWCQDNGVLLHIHRAMHAVID
RNPNHGIHFRVLTKILRLSGGDHLHTGTVVGKLEGDRAST
LGWIDLLRESFIPEDRSRGIFFDQDWGSMPGVFAVASGGI
HVWHMPALVNIFGDDSVLQFGGGTLGHPWGNAAGAAANRV
ALEACVEARNQGRDIEKEGKEILTAAAQHSPELKIAMETW
KEIKF
M:  EMQDYKQSLKYETFSYLPPMNAERIRAQIKYAIAQGWSPG
IEHVEVKNSMNQYWYMWKLPFFGEQNVDNVLAEIEACRSA
YPTHQVKLVAYDNYAQSLGLAFVVYRGN
Description


Functional site

1) chain A
residue 288
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 474
source : AC1

2) chain A
residue 320
type
sequence H
description BINDING SITE FOR RESIDUE SO4 A 474
source : AC1

3) chain A
residue 372
type
sequence S
description BINDING SITE FOR RESIDUE SO4 A 474
source : AC1

4) chain A
residue 374
type
sequence G
description BINDING SITE FOR RESIDUE SO4 A 475
source : AC2

5) chain A
residue 396
type
sequence G
description BINDING SITE FOR RESIDUE SO4 A 475
source : AC2

6) chain A
residue 397
type
sequence G
description BINDING SITE FOR RESIDUE SO4 A 475
source : AC2

7) chain A
residue 156
type
sequence N
description BINDING SITE FOR RESIDUE GOL M 111
source : AC3

8) chain M
residue 13
type
sequence Y
description BINDING SITE FOR RESIDUE GOL M 111
source : AC3

9) chain M
residue 51
type
sequence S
description BINDING SITE FOR RESIDUE GOL M 111
source : AC3

10) chain M
residue 89
type
sequence K
description BINDING SITE FOR RESIDUE GOL M 111
source : AC3

11) chain A
residue 189-197
type prosite
sequence GLDFTKDDE
description RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE
source prosite : PS00157

12) chain A
residue 168
type ACT_SITE
sequence K
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 287
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 116
type BINDING
sequence N
description in homodimeric partner => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI2

15) chain A
residue 166
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI3

16) chain A
residue 170
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI3

17) chain A
residue 196
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI3

18) chain A
residue 197
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI3

19) chain A
residue 288
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI3

20) chain A
residue 320
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI3

21) chain A
residue 372
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI3

22) chain A
residue 194
type BINDING
sequence K
description via carbamate group => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI4

23) chain A
residue 327
type SITE
sequence K
description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI5

24) chain A
residue 194
type MOD_RES
sequence K
description N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01338
source Swiss-Prot : SWS_FT_FI6


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