eF-site ID 3vm6-ABC
PDB Code 3vm6
Chain A, B, C

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Title Crystal structure of ribose-1,5-bisphosphate isomerase from Thermococcus kodakarensis KOD1 in complex with alpha-D-ribose-1,5-bisphosphate
Classification ISOMERASE
Compound Translation initiation factor eIF-2B, delta subunit
Source (Q5JFM9_PYRKO)
Sequence A:  AVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKSK
ATNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRGK
IAYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGAK
RIEDGDVIMTHSHSKAAISVMKTAWEQGKDIKVIVTETRP
KWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMGA
DSITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFHP
ETMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFDV
TPPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPWE
D
B:  AVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKSK
ATNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRGK
IAYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGAK
RIEDGDVIMTHSHSKAAISVMKTAWEQGKDIKVIVTETRP
KWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMGA
DSITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFHP
ETMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFDV
TPPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPWE
D
C:  AVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKSK
ATNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRGK
IAYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGAK
RIEDGDVIMTHSHSKAAISVMKTAWEQGKDIKVIVTETRP
KWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMGA
DSITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFHP
ETMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFDV
TPPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPWE
D
Description


Functional site

1) chain A
residue 133
type ACT_SITE
sequence S
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 133
type ACT_SITE
sequence S
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI1

3) chain C
residue 133
type ACT_SITE
sequence S
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI1

4) chain A
residue 202
type ACT_SITE
sequence D
description Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI2

5) chain B
residue 202
type ACT_SITE
sequence D
description Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI2

6) chain C
residue 202
type ACT_SITE
sequence D
description Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI2

7) chain A
residue 20
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230
source Swiss-Prot : SWS_FT_FI3

8) chain A
residue 135
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230
source Swiss-Prot : SWS_FT_FI3

9) chain A
residue 212
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230
source Swiss-Prot : SWS_FT_FI3

10) chain B
residue 20
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230
source Swiss-Prot : SWS_FT_FI3

11) chain B
residue 135
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230
source Swiss-Prot : SWS_FT_FI3

12) chain B
residue 212
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230
source Swiss-Prot : SWS_FT_FI3

13) chain C
residue 20
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230
source Swiss-Prot : SWS_FT_FI3

14) chain C
residue 135
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230
source Swiss-Prot : SWS_FT_FI3

15) chain C
residue 212
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230
source Swiss-Prot : SWS_FT_FI3

16) chain A
residue 63
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI4

17) chain A
residue 238
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI4

18) chain B
residue 63
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI4

19) chain B
residue 238
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI4

20) chain C
residue 63
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI4

21) chain C
residue 238
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789
source Swiss-Prot : SWS_FT_FI4

22) chain A
residue 227
type SITE
sequence R
description Plays a key role in hexamerization
source Swiss-Prot : SWS_FT_FI5

23) chain B
residue 227
type SITE
sequence R
description Plays a key role in hexamerization
source Swiss-Prot : SWS_FT_FI5

24) chain C
residue 227
type SITE
sequence R
description Plays a key role in hexamerization
source Swiss-Prot : SWS_FT_FI5


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