eF-site ID 1ide-A
PDB Code 1ide
Chain A

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Title ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)
Classification OXIDOREDUCTASE (NAD(A)-CHOH(D))
Compound ISOCITRATE DEHYDROGENASE
Source Escherichia coli (strain K12) (IDH_ECOLI)
Sequence A:  SKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVT
PAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQDV
WLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQEL
DLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIFAG
IEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPCS
EEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFK
DWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIA
DAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGIGI
APGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAEM
MLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAKL
LKCSEFGDAIIENM
Description


Functional site
1) chain A
residue 113
type
sequence S
description ISOCITRATE/MG++ BINDING SITE
source : SUB
2) chain A
residue 115
type
sequence N
description ISOCITRATE/MG++ BINDING SITE
source : SUB
3) chain A
residue 119
type
sequence R
description ISOCITRATE/MG++ BINDING SITE
source : SUB
4) chain A
residue 129
type
sequence R
description ISOCITRATE/MG++ BINDING SITE
source : SUB
5) chain A
residue 153
type
sequence R
description ISOCITRATE/MG++ BINDING SITE
source : SUB
6) chain A
residue 160
type
sequence F
description ISOCITRATE/MG++ BINDING SITE
source : SUB
7) chain A
residue 307
type
sequence D
description ISOCITRATE/MG++ BINDING SITE
source : SUB
8) chain A
residue 311
type
sequence D
description ISOCITRATE/MG++ BINDING SITE
source : SUB
9) chain A
residue 283
type
sequence D
description BINDING SITE FOR RESIDUE MG A 417
source : AC1
10) chain A
residue 307
type
sequence D
description BINDING SITE FOR RESIDUE MG A 417
source : AC1
11) chain A
residue 311
type
sequence D
description BINDING SITE FOR RESIDUE MG A 417
source : AC1
12) chain A
residue 119
type
sequence R
description BINDING SITE FOR RESIDUE ICT A 418
source : AC2
13) chain A
residue 129
type
sequence R
description BINDING SITE FOR RESIDUE ICT A 418
source : AC2
14) chain A
residue 153
type
sequence R
description BINDING SITE FOR RESIDUE ICT A 418
source : AC2
15) chain A
residue 160
type
sequence F
description BINDING SITE FOR RESIDUE ICT A 418
source : AC2
16) chain A
residue 232
type
sequence N
description BINDING SITE FOR RESIDUE ICT A 418
source : AC2
17) chain A
residue 283
type
sequence D
description BINDING SITE FOR RESIDUE ICT A 418
source : AC2
18) chain A
residue 307
type
sequence D
description BINDING SITE FOR RESIDUE ICT A 418
source : AC2
19) chain A
residue 37
type
sequence I
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
20) chain A
residue 102
type
sequence P
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
21) chain A
residue 103
type
sequence L
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
22) chain A
residue 104
type
sequence T
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
23) chain A
residue 115
type
sequence N
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
24) chain A
residue 337
type
sequence A
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
25) chain A
residue 338
type
sequence T
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
26) chain A
residue 339
type
sequence H
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
27) chain A
residue 340
type
sequence G
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
28) chain A
residue 342
type
sequence A
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
29) chain A
residue 343
type
sequence P
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
30) chain A
residue 345
type
sequence Y
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
31) chain A
residue 351
type
sequence V
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
32) chain A
residue 352
type
sequence N
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
33) chain A
residue 391
type
sequence Y
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
34) chain A
residue 392
type
sequence D
description BINDING SITE FOR RESIDUE NAP A 419
source : AC3
35) chain A
residue 160
type catalytic
sequence F
description 7
source MCSA : MCSA1
36) chain A
residue 230
type catalytic
sequence K
description 7
source MCSA : MCSA1
37) chain A
residue 283
type catalytic
sequence D
description 7
source MCSA : MCSA1
38) chain A
residue 307
type catalytic
sequence D
description 7
source MCSA : MCSA1
39) 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
40) chain A
residue 303-322
type prosite
sequence NLNGDYISDALAAQVGGIGI
description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYiSDalAaqv.GGIGI
source prosite : PS00470
41) chain A
residue 113
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:3112144
source Swiss-Prot : SWS_FT_FI10
42) chain A
residue 142
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI11
43) 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
44) 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
45) 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
46) 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
47) 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
48) 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
49) chain A
residue 160
type SITE
sequence F
description Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221
source Swiss-Prot : SWS_FT_FI8
50) 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
51) chain A
residue 100
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI9
52) chain A
residue 242
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:21151122
source Swiss-Prot : SWS_FT_FI9
53) chain A
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
54) 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
55) 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
56) 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

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