|
eF-site ID
|
1ika-A |
PDB Code
|
1ika |
Chain
|
A |
|
click to enlarge
|
|
Title
|
STRUCTURE OF ISOCITRATE DEHYDROGENASE WITH ALPHA-KETOGLUTARATE AT 2.7 ANGSTROMS RESOLUTION: CONFORMATIONAL CHANGES INDUCED BY DECARBOXYLATION OF ISOCITRATE |
Classification
|
OXIDOREDUCTASE(NAD(A)-CHOH(D)) |
Compound
|
ISOCITRATE DEHYDROGENASE |
Source
|
(IDH_ECOLI) |
|
Sequence
|
A: |
SKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVT
PAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQDV
WLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQEL
DLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYAG
IEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPCS
EEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFK
DWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIA
DAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGIGI
APGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAEM
MLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAKL
LKCSEFGDAIIENM
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
307 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE CA A 417
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
311 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE CA A 417
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
113 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE AKG A 418
|
source |
: AC2
|
|
4)
|
chain |
A |
residue |
115 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE AKG A 418
|
source |
: AC2
|
|
5)
|
chain |
A |
residue |
119 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE AKG A 418
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
129 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE AKG A 418
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
230 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE AKG A 418
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
283 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE AKG A 418
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
307 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE AKG A 418
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
311 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE AKG A 418
|
source |
: AC2
|
|
11)
|
chain |
A |
residue |
160 |
type |
catalytic |
sequence |
Y
|
description |
7
|
source |
MCSA : MCSA1
|
|
12)
|
chain |
A |
residue |
230 |
type |
catalytic |
sequence |
K
|
description |
7
|
source |
MCSA : MCSA1
|
|
13)
|
chain |
A |
residue |
283 |
type |
catalytic |
sequence |
D
|
description |
7
|
source |
MCSA : MCSA1
|
|
14)
|
chain |
A |
residue |
307 |
type |
catalytic |
sequence |
D
|
description |
7
|
source |
MCSA : MCSA1
|
|
15)
|
chain |
A |
residue |
303-322 |
type |
prosite |
sequence |
NLNGDYISDALAAQVGGIGI
|
description |
IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYiSDalAaqv.GGIGI
|
source |
prosite : PS00470
|
|
16)
|
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
|
|
17)
|
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
|
|
18)
|
chain |
A |
residue |
142 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0000269|PubMed:18723842
|
source |
Swiss-Prot : SWS_FT_FI11
|
|
19)
|
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
|
|
20)
|
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
|
|
21)
|
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
|
|
22)
|
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
|
|
23)
|
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
|
|
24)
|
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
|
|
25)
|
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
|
|
26)
|
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
|
|
27)
|
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
|
|
28)
|
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
|
|
29)
|
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
|
|
30)
|
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
|
|
31)
|
chain |
A |
residue |
100 |
type |
MOD_RES |
sequence |
K
|
description |
N6-succinyllysine => ECO:0000269|PubMed:21151122
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
32)
|
chain |
A |
residue |
242 |
type |
MOD_RES |
sequence |
K
|
description |
N6-succinyllysine => ECO:0000269|PubMed:21151122
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
|
|