eF-site ID 4icd-A
PDB Code 4icd
Chain A

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Title REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME
Classification OXIDOREDUCTASE (NAD(A)-CHOH(D))
Compound PHOSPHORYLATED ISOCITRATE DEHYDROGENASE
Source Escherichia coli (strain K12) (IDH_ECOLI)
Sequence A:  SKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVT
PAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQDV
WLPAETLDLIREYRVAIKGPLTTPVGGGIRXLNVALRQEL
DLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYAG
IEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPCS
EEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFK
DWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIA
DAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGIGI
APGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAEM
MLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAKL
LKCSEFGDAIIENM
Description (1)  PHOSPHORYLATED ISOCITRATE DEHYDROGENASE (E.C.1.1.1.42)


Functional site
1) chain A
residue 160
type catalytic
sequence Y
description 7
source MCSA : MCSA1
2) chain A
residue 230
type catalytic
sequence K
description 7
source MCSA : MCSA1
3) chain A
residue 283
type catalytic
sequence D
description 7
source MCSA : MCSA1
4) chain A
residue 307
type catalytic
sequence D
description 7
source MCSA : MCSA1
5) chain A
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 A
residue 113
type MOD_RES
sequence X
description Phosphoserine => ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:3112144
source Swiss-Prot : SWS_FT_FI10
7) chain A
residue 142
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI11
8) chain A
residue 303-322
type prosite
sequence NLNGDYISDALAAQVGGIGI
description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYiSDalAaqv.GGIGI
source prosite : PS00470
9) chain A
residue 113
type BINDING
sequence X
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 A
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
11) chain A
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
12) chain A
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
13) chain A
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
14) chain A
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
15) chain A
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
16) chain A
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
17) chain A
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
18) chain A
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
19) chain A
residue 160
type SITE
sequence Y
description Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221
source Swiss-Prot : SWS_FT_FI8
20) chain A
residue 230
type SITE
sequence K
description Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221
source Swiss-Prot : SWS_FT_FI8
21) chain A
residue 100
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI9
22) chain A
residue 242
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI9

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