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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