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4AOU

CtIDH bound to NADP. The complex structures of Isocitrate dehydrogenase from Clostridium thermocellum and Desulfotalea psychrophila, support a new active site locking mechanism

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
A0006099biological_processtricarboxylic acid cycle
A0006102biological_processisocitrate metabolic process
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
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAP A 1520
ChainResidue
ATHR75
ATHR308
AVAL309
ATHR310
AARG311
AHIS312
AASN325
AICT1403
AHOH2032
AHOH2040
ATHR77
AARG82
AASP251
AARG255
ALEU286
AALA287
AHIS306
AGLY307

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ICT A 1403
ChainResidue
ATHR77
ASER94
AASN96
AARG100
AARG109
AARG132
ATYR139
ALYS210
AILE213
AASP250
AASP273
AALA305
AMG1404
ANAP1520
AHOH2029

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 1404
ChainResidue
AASP250
AASP273
AICT1403
AHOH2029

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVmSDmvAsaf.GSLAM
ChainResidueDetails
AASN269-MET288

222624

PDB entries from 2024-07-17

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