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6VH5

Crystal structure of prephenate dehydratase from brucella melitensis biovar abortus 2308 in complex with phenylalanine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004106molecular_functionchorismate mutase activity
A0004664molecular_functionprephenate dehydratase activity
A0005737cellular_componentcytoplasm
A0009094biological_processL-phenylalanine biosynthetic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
B0004106molecular_functionchorismate mutase activity
B0004664molecular_functionprephenate dehydratase activity
B0005737cellular_componentcytoplasm
B0009094biological_processL-phenylalanine biosynthetic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
C0004106molecular_functionchorismate mutase activity
C0004664molecular_functionprephenate dehydratase activity
C0005737cellular_componentcytoplasm
C0009094biological_processL-phenylalanine biosynthetic process
C0016829molecular_functionlyase activity
C0016836molecular_functionhydro-lyase activity
D0004106molecular_functionchorismate mutase activity
D0004664molecular_functionprephenate dehydratase activity
D0005737cellular_componentcytoplasm
D0009094biological_processL-phenylalanine biosynthetic process
D0016829molecular_functionlyase activity
D0016836molecular_functionhydro-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue PHE A 301
ChainResidue
AASN222
CTHR238
CPHE240
CEDO302
AMET223
ATHR224
ALYS225
CASN204
CVAL205
CALA207
CALA208
CLEU209

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 302
ChainResidue
AALA207
ALEU209
ATYR210
CPHE216
CVAL221
CPHE301

site_idAC3
Number of Residues12
Detailsbinding site for residue PHE B 301
ChainResidue
BASN222
BMET223
BTHR224
BLYS225
DASN204
DVAL205
DALA208
DLEU209
DSER228
DTHR238
DPHE240
DEDO302

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO B 302
ChainResidue
BALA207
BALA208
BLEU209
BTYR210
DPHE216
DVAL221
DPHE301

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO B 303
ChainResidue
BLEU109
BGLY123

site_idAC6
Number of Residues12
Detailsbinding site for residue PHE C 301
ChainResidue
AASN204
AVAL205
AALA207
AALA208
ALEU209
ATHR238
APHE240
AEDO302
CASN222
CMET223
CTHR224
CLYS225

site_idAC7
Number of Residues7
Detailsbinding site for residue EDO C 302
ChainResidue
APHE216
AVAL221
APHE301
CALA207
CALA208
CLEU209
CTYR210

site_idAC8
Number of Residues12
Detailsbinding site for residue PHE D 301
ChainResidue
BASN204
BVAL205
BALA207
BALA208
BLEU209
BTHR238
BPHE240
BEDO302
DASN222
DMET223
DTHR224
DLYS225

site_idAC9
Number of Residues8
Detailsbinding site for residue EDO D 302
ChainResidue
BPHE216
BALA217
BVAL221
BPHE301
DALA207
DALA208
DLEU209
DTYR210

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO D 303
ChainResidue
DHIS66
DTYR229
DLEU231
DGLN239
DHOH416

Functional Information from PROSITE/UniProt
site_idPS00857
Number of Residues23
DetailsPREPHENATE_DEHYDR_1 Prephenate dehydratase signature 1. YgLdiLeenveDsennvTRFVvL
ChainResidueDetails
ATYR156-LEU178

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PDB entries from 2024-10-09

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