Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2D4V

Crystal structure of NAD dependent isocitrate dehydrogenase from Acidithiobacillus thiooxidans

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
C0006097biological_processglyoxylate cycle
C0006099biological_processtricarboxylic acid cycle
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0046872molecular_functionmetal ion binding
C0051287molecular_functionNAD binding
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
D0006097biological_processglyoxylate cycle
D0006099biological_processtricarboxylic acid cycle
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0046872molecular_functionmetal ion binding
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FLC A 3001
ChainResidue
ATHR105
AHOH3164
BLYS230
BASN232
BASP296
ASER113
AASN115
AARG119
AARG129
AARG153
ATYR160
AASP320
ANAD2001

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FLC B 3101
ChainResidue
ALYS230
AASN232
AILE233
BTHR105
BSER113
BASN115
BARG119
BARG129
BARG153
BTYR160
BASP320
BNAD2101
BHOH3150

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FLC C 3201
ChainResidue
CTHR105
CSER113
CASN115
CARG119
CARG129
CARG153
CTYR160
CASP320
CNAD2201
CHOH3247
DLYS230
DASN232
DILE233
DASP296

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE FLC D 3301
ChainResidue
CLYS230
CASN232
CILE233
CASP296
CHOH3279
DTHR105
DSER113
DASN115
DARG119
DARG129
DARG153
DTYR160
DASP320
DNAD2301
DHOH3552

site_idAC5
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAD A 2001
ChainResidue
AILE37
ALYS100
APRO102
ALEU103
AGLU104
ATHR105
AASN115
AILE333
AGLU349
ATHR351
AHIS352
AGLY353
ATHR354
AALA355
AASP357
AALA364
AASN365
AASP405
AFLC3001
AHOH3016
AHOH3038
AHOH3070
AHOH3108
AHOH3125
AHOH3151
AHOH3171
AHOH3186
BASN232
BILE294
BASN297
BGLN300

site_idAC6
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAD B 2101
ChainResidue
BGLU349
BTHR351
BHIS352
BGLY353
BTHR354
BALA355
BASP357
BALA364
BASN365
BASP405
BFLC3101
BHOH3130
BHOH3133
BHOH3151
BHOH3165
BHOH3271
BHOH3314
AASN232
AILE294
AASN297
AGLN300
AHOH3058
AHOH3060
BILE37
BLYS100
BPRO102
BLEU103
BTHR105
BASN115
BILE333

site_idAC7
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAD C 2201
ChainResidue
CILE37
CLYS100
CPRO102
CLEU103
CGLU104
CTHR105
CASN115
CILE333
CGLU349
CTHR351
CHIS352
CGLY353
CTHR354
CALA355
CASP357
CALA364
CASN365
CASP405
CFLC3201
CHOH3210
CHOH3227
CHOH3330
CHOH3336
CHOH3362
CHOH3421
DASN232
DILE294
DASN297
DGLN300
DHOH3346
DHOH3407

site_idAC8
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAD D 2301
ChainResidue
CASN232
CILE294
CASN297
CGLN300
CHOH3248
DILE37
DLYS100
DPRO102
DLEU103
DGLU104
DTHR105
DASN115
DILE333
DGLU349
DTHR351
DHIS352
DGLY353
DTHR354
DALA355
DASP357
DALA364
DASN365
DASP405
DFLC3301
DHOH3307
DHOH3360
DHOH3366
DHOH3442
DHOH3574
DHOH3625

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYvSDalAaev.GGIGM
ChainResidueDetails
AASN316-MET335

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
AASP296
ALYS230
BTYR160

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ATYR160
BASP296
BLYS230

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
DTYR160
CASP296
CLYS230

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
CTYR160
DASP296
DLYS230

225158

PDB entries from 2024-09-18

PDB statisticsPDBj update infoContact PDBjnumon