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4HCX

Structure of ICDH-1 from M.tuberculosis complexed with NADPH & Mn2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0006102biological_processisocitrate metabolic process
A0008270molecular_functionzinc ion binding
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
B0000287molecular_functionmagnesium ion binding
B0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0006102biological_processisocitrate metabolic process
B0008270molecular_functionzinc ion binding
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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 501
ChainResidue
AASP278
AASP282
AHOH708
BASP255
BHOH604

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NDP A 502
ChainResidue
ATHR80
AARG85
AGLU309
AHIS312
AGLY313
ATHR314
AVAL315
ATHR316
AARG317
AHIS318
ATHR330
AASN331
AHOH608
AHOH610
AHOH612
AHOH724
AHOH754
ALYS75
AALA77
ATHR78
AILE79

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
AGLY139
AARG143

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 501
ChainResidue
AASP255
AHOH607
BASP278
BASP282
BHOH720

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NDP B 502
ChainResidue
BLYS75
BALA77
BTHR78
BTHR80
BARG85
BASN99
BGLU309
BHIS312
BGLY313
BTHR314
BVAL315
BTHR316
BHIS318
BTHR330
BASN331
BHOH606
BHOH686
BHOH702
BHOH707

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 503
ChainResidue
BPHE138
BGLY139
BARG143
BHOH658

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDtvAqgy.GSLGL
ChainResidueDetails
AASN274-LEU293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23409873","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HCX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsSite: {"description":"Critical for catalysis","evidences":[{"source":"UniProtKB","id":"P08200","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"28250431","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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