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6IXT

Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri in complex with NAD+ and Mg2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
A0006102biological_processisocitrate metabolic process
B0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
B0006102biological_processisocitrate metabolic process
C0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
C0006102biological_processisocitrate metabolic process
D0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
D0006102biological_processisocitrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue NAD A 501
ChainResidue
AHIS339
AHOH682
AHOH708
AHOH744
AGLY340
ATHR341
AVAL342
AASP344
AMET345
AASN358
AGOL503
AHOH613

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
AASP302
AASP306
AHOH710
BASP278
BHOH747

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 503
ChainResidue
AGLY316
APHE317
AASN358
ALEU360
AGLY361
ANAD501
AHOH613
AHOH637

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 504
ChainResidue
AGLY119
AARG123
AHOH673
AHOH727

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 505
ChainResidue
AASP380
AARG381
AASP382
AHOH696

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL B 501
ChainResidue
BTYR230
BTRP287
BGLN289
BGLY290

site_idAC7
Number of Residues5
Detailsbinding site for residue SO4 B 502
ChainResidue
BASN118
BARG122
BARG152
BTYR159
BASP302

site_idAC8
Number of Residues7
Detailsbinding site for residue SO4 B 503
ChainResidue
BHIS339
BGLY340
BTHR341
BVAL342
BHOH784
BHOH785
BHOH786

site_idAC9
Number of Residues10
Detailsbinding site for residue NAD C 501
ChainResidue
CHIS339
CGLY340
CTHR341
CVAL342
CASP344
CMET345
CLEU357
CASN358
CHOH620
CHOH708

site_idAD1
Number of Residues3
Detailsbinding site for residue GOL C 502
ChainResidue
CTYR230
CGLY290
CHOH770

site_idAD2
Number of Residues5
Detailsbinding site for residue SO4 C 503
ChainResidue
CASP380
CARG381
CASP382
CHOH686
CHOH768

site_idAD3
Number of Residues3
Detailsbinding site for residue SO4 C 504
ChainResidue
CASN118
CARG122
CARG152

site_idAD4
Number of Residues7
Detailsbinding site for residue GOL D 501
ChainResidue
CASP278
DARG132
DASP302
DTHR305
DASP306
DSO4503
DHOH737

site_idAD5
Number of Residues6
Detailsbinding site for residue SO4 D 502
ChainResidue
DHIS339
DGLY340
DTHR341
DVAL342
DHOH644
DHOH695

site_idAD6
Number of Residues7
Detailsbinding site for residue SO4 D 503
ChainResidue
CLYS234
DASN118
DARG122
DARG152
DTYR159
DASP302
DGOL501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|Ref.4, ECO:0007744|PDB:6IXN
ChainResidueDetails
ATHR97
CASN118
CLYS283
CHIS339
DTHR97
DASN118
DLYS283
DHIS339
AASN118
ALYS283
AHIS339
BTHR97
BASN118
BLYS283
BHIS339
CTHR97

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|Ref.4, ECO:0007744|PDB:7E2W
ChainResidueDetails
ASER116
CARG152
CTYR159
CLYS234
DSER116
DARG152
DTYR159
DLYS234
AARG152
ATYR159
ALYS234
BSER116
BARG152
BTYR159
BLYS234
CSER116

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|Ref.4, ECO:0007744|PDB:6IXT
ChainResidueDetails
AASP278
DASP278
DASP302
DASP306
AASP302
AASP306
BASP278
BASP302
BASP306
CASP278
CASP302
CASP306

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.4, ECO:0007744|PDB:6IXN, ECO:0007744|PDB:6IXT
ChainResidueDetails
AASN358
BASN358
CASN358
DASN358

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PDB entries from 2025-07-02

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