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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
A0009800biological_processcinnamic acid biosynthetic process
A0016841molecular_functionammonia-lyase activity
A0045548molecular_functionphenylalanine ammonia-lyase activity
A0052883molecular_functiontyrosine ammonia-lyase activity
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0006559biological_processL-phenylalanine catabolic process
B0009800biological_processcinnamic acid biosynthetic process
B0016841molecular_functionammonia-lyase activity
B0045548molecular_functionphenylalanine ammonia-lyase activity
B0052883molecular_functiontyrosine ammonia-lyase activity
C0003824molecular_functioncatalytic activity
C0005737cellular_componentcytoplasm
C0006559biological_processL-phenylalanine catabolic process
C0009800biological_processcinnamic acid biosynthetic process
C0016841molecular_functionammonia-lyase activity
C0045548molecular_functionphenylalanine ammonia-lyase activity
C0052883molecular_functiontyrosine ammonia-lyase activity
D0003824molecular_functioncatalytic activity
D0005737cellular_componentcytoplasm
D0006559biological_processL-phenylalanine catabolic process
D0009800biological_processcinnamic acid biosynthetic process
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 Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q68G84","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15350127","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T6J","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"2,3-didehydroalanine (Ser)","evidences":[{"source":"PubMed","id":"15350127","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsCross-link: {"description":"5-imidazolinone (Ala-Gly)","evidences":[{"source":"PubMed","id":"15350127","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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 2026-03-25

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