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5ZE4

The structure of holo- structure of DHAD complex with [2Fe-2S] cluster

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004160molecular_functiondihydroxy-acid dehydratase activity
A0005507molecular_functioncopper ion binding
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009082biological_processbranched-chain amino acid biosynthetic process
A0009097biological_processisoleucine biosynthetic process
A0009099biological_processvaline biosynthetic process
A0009507cellular_componentchloroplast
A0009536cellular_componentplastid
A0009553biological_processembryo sac development
A0009555biological_processpollen development
A0009570cellular_componentchloroplast stroma
A0009651biological_processresponse to salt stress
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0046872molecular_functionmetal ion binding
A0048364biological_processroot development
A0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue FES A 601
ChainResidue
ACYS66
AASP98
AALA99
ACYS139
AASP140
ACYS211
AALA217
AACT605

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 602
ChainResidue
ATHR104
AARG105
ATRP129
AARG25

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 603
ChainResidue
AASN17
APRO29
ALYS30
ASER31
ATYR184

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 604
ChainResidue
ASER45
AASP46
AHIS202
AHOH804

site_idAC5
Number of Residues3
Detailsbinding site for residue ACT A 605
ChainResidue
ACYS211
ATYR215
AFES601

site_idAC6
Number of Residues4
Detailsbinding site for residue MG A 606
ChainResidue
AASP98
AASP140
ALYS141
AGLU463

Functional Information from PROSITE/UniProt
site_idPS00886
Number of Residues11
DetailsILVD_EDD_1 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. CDKnmPGtimA
ChainResidueDetails
ACYS139-ALA149

site_idPS00887
Number of Residues12
DetailsILVD_EDD_2 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 2. ALLTDGRFSGGS
ChainResidueDetails
AALA481-SER492

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P9WKJ5
ChainResidueDetails
ASER489

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:29995859, ECO:0007744|PDB:5ZE4
ChainResidueDetails
ACYS66
ACYS139
AASP140
ACYS211
AGLU463

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WKJ5
ChainResidueDetails
AASP98

222415

PDB entries from 2024-07-10

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