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3MWB

The Crystal Structure of Prephenate dehydratase in complex with L-Phe from Arthrobacter aurescens to 2.0A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004106molecular_functionchorismate mutase activity
A0004664molecular_functionprephenate dehydratase activity
A0009094biological_processL-phenylalanine biosynthetic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0046872molecular_functionmetal ion binding
B0004106molecular_functionchorismate mutase activity
B0004664molecular_functionprephenate dehydratase activity
B0009094biological_processL-phenylalanine biosynthetic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PHE B 311
ChainResidue
AASN226
BALA212
BLEU213
BPHE244
BHOH447
ALEU227
ASER228
AARG229
AILE230
AHOH442
BASP208
BHIS209
BGLY211

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PHE B 312
ChainResidue
AASP208
AHIS209
AGLY211
AALA212
ALEU213
ASER232
APHE244
BASN226
BLEU227
BSER228
BARG229
BILE230
BHOH438
BHOH439

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 313
ChainResidue
BALA158
BGLN161
BLEU164

Functional Information from PROSITE/UniProt
site_idPS00858
Number of Residues8
DetailsPREPHENATE_DEHYDR_2 Prephenate dehydratase signature 2. LSRIESRP
ChainResidueDetails
ALEU227-PRO234

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PDB entries from 2024-07-10

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