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5YM0

The crystal structure of DHAD

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 Residues4
Detailsbinding site for residue SO4 A 701
ChainResidue
AARG59
ATHR138
AARG139
ATRP163

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 A 702
ChainResidue
AHOH827
AHOH836
AHOH907
AASN98
ASER131
AASP132
AALA133
AASP174

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 703
ChainResidue
ALYS175
ATYR249
ATHR250
AASN323
AGLU497
ASER523
AHOH801

Functional Information from PROSITE/UniProt
site_idPS00886
Number of Residues11
DetailsILVD_EDD_1 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. CDKnmPGtimA
ChainResidueDetails
ACYS173-ALA183

site_idPS00887
Number of Residues12
DetailsILVD_EDD_2 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 2. ALLTDGRFSGGS
ChainResidueDetails
AALA515-SER526

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P9WKJ5
ChainResidueDetails
ASER523

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:29995859, ECO:0007744|PDB:5ZE4
ChainResidueDetails
ACYS173
ACYS245
AGLU497
AASP174
ACYS100

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WKJ5
ChainResidueDetails
AASP132

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22223895
ChainResidueDetails
ASER35

221051

PDB entries from 2024-06-12

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