eF-site ID 3lcb-D
PDB Code 3lcb
Chain D

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Title The crystal structure of isocitrate dehydrogenase kinase/phosphatase in complex with its substrate, isocitrate dehydrogenase, from Escherichia coli.
Classification TRANSFERASE, HYDROLASE
Compound Isocitrate dehydrogenase kinase/phosphatase
Source Escherichia coli O157:H7 (strain EC4115 / EHEC) (IDH_ECOLI)
Sequence D:  ESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDV
TPAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQD
VWLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQE
LDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYA
GIEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPC
SEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAF
KDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVI
ADAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGIG
IAPGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAE
MMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAK
LLKCSEFGDAIIENM
Description


Functional site

1) chain D
residue 160
type catalytic
sequence Y
description 7
source MCSA : MCSA2

2) chain D
residue 230
type catalytic
sequence K
description 7
source MCSA : MCSA2

3) chain D
residue 283
type catalytic
sequence D
description 7
source MCSA : MCSA2

4) chain D
residue 307
type catalytic
sequence D
description 7
source MCSA : MCSA2

5) chain D
residue 104
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR
source Swiss-Prot : SWS_FT_FI1

6) chain D
residue 113
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:3112144
source Swiss-Prot : SWS_FT_FI10

7) chain D
residue 142
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI11

8) chain D
residue 113
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD
source Swiss-Prot : SWS_FT_FI2

9) chain D
residue 115
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD
source Swiss-Prot : SWS_FT_FI2

10) chain D
residue 129
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD
source Swiss-Prot : SWS_FT_FI2

11) chain D
residue 153
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD
source Swiss-Prot : SWS_FT_FI2

12) chain D
residue 119
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD
source Swiss-Prot : SWS_FT_FI3

13) chain D
residue 307
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDC, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:8ICD
source Swiss-Prot : SWS_FT_FI4

14) chain D
residue 339
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:1ISO, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD
source Swiss-Prot : SWS_FT_FI5

15) chain D
residue 352
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD
source Swiss-Prot : SWS_FT_FI6

16) chain D
residue 391
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD
source Swiss-Prot : SWS_FT_FI6

17) chain D
residue 395
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:9ICD
source Swiss-Prot : SWS_FT_FI7

18) chain D
residue 160
type SITE
sequence Y
description Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221
source Swiss-Prot : SWS_FT_FI8

19) chain D
residue 230
type SITE
sequence K
description Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221
source Swiss-Prot : SWS_FT_FI8

20) chain D
residue 100
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI9

21) chain D
residue 242
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI9


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