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1Y2M

Crystal structure of phenylalanine ammonia-lyase from yeast Rhododporidium toruloides

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0006559biological_processL-phenylalanine catabolic process
A0009698biological_processphenylpropanoid metabolic process
A0009800biological_processcinnamic acid biosynthetic process
A0016829molecular_functionlyase activity
A0016841molecular_functionammonia-lyase activity
A0045548molecular_functionphenylalanine ammonia-lyase activity
A0052883molecular_functiontyrosine ammonia-lyase activity
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0006559biological_processL-phenylalanine catabolic process
B0009698biological_processphenylpropanoid metabolic process
B0009800biological_processcinnamic acid biosynthetic process
B0016829molecular_functionlyase activity
B0016841molecular_functionammonia-lyase activity
B0045548molecular_functionphenylalanine ammonia-lyase activity
B0052883molecular_functiontyrosine ammonia-lyase activity
C0003824molecular_functioncatalytic activity
C0005737cellular_componentcytoplasm
C0006559biological_processL-phenylalanine catabolic process
C0009698biological_processphenylpropanoid metabolic process
C0009800biological_processcinnamic acid biosynthetic process
C0016829molecular_functionlyase activity
C0016841molecular_functionammonia-lyase activity
C0045548molecular_functionphenylalanine ammonia-lyase activity
C0052883molecular_functiontyrosine ammonia-lyase activity
D0003824molecular_functioncatalytic activity
D0005737cellular_componentcytoplasm
D0006559biological_processL-phenylalanine catabolic process
D0009698biological_processphenylpropanoid metabolic process
D0009800biological_processcinnamic acid biosynthetic process
D0016829molecular_functionlyase activity
D0016841molecular_functionammonia-lyase activity
D0045548molecular_functionphenylalanine ammonia-lyase activity
D0052883molecular_functiontyrosine ammonia-lyase activity
Functional Information from PROSITE/UniProt
site_idPS00488
Number of Residues17
DetailsPAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GTISASGDLsPLSyiaA
ChainResidueDetails
AGLY207-ALA223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q68G84
ChainResidueDetails
ATYR110
BTYR110
CTYR110
DTYR110

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q68G84
ChainResidueDetails
AASN270
BASN499
CASN270
CGLN360
CARG366
CASN397
CASN499
DASN270
DGLN360
DARG366
DASN397
AGLN360
DASN499
AARG366
AASN397
AASN499
BASN270
BGLN360
BARG366
BASN397

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15350127, ECO:0007744|PDB:1T6J
ChainResidueDetails
ALYS468
AGLU496
BLYS468
BGLU496
CLYS468
CGLU496
DLYS468
DGLU496

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: 2,3-didehydroalanine (Ser) => ECO:0000269|PubMed:15350127
ChainResidueDetails
ASER212
BSER212
CSER212
DSER212

site_idSWS_FT_FI5
Number of Residues8
DetailsCROSSLNK: 5-imidazolinone (Ala-Gly) => ECO:0000269|PubMed:15350127
ChainResidueDetails
AALA211
AGLY213
BALA211
BGLY213
CALA211
CGLY213
DALA211
DGLY213

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1b8f
ChainResidueDetails
ASER212
AGLN500
AALA211
AGLY213
ATYR363

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1b8f
ChainResidueDetails
BSER212
BGLN500
BALA211
BGLY213
BTYR363

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1b8f
ChainResidueDetails
CSER212
CGLN500
CALA211
CGLY213
CTYR363

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1b8f
ChainResidueDetails
DSER212
DGLN500
DALA211
DGLY213
DTYR363

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PDB entries from 2024-07-24

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