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1W27

Phenylalanine ammonia-lyase (PAL) from Petroselinum crispum

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
A0016597molecular_functionamino acid binding
A0016829molecular_functionlyase activity
A0016841molecular_functionammonia-lyase activity
A0032991cellular_componentprotein-containing complex
A0045548molecular_functionphenylalanine ammonia-lyase activity
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0006559biological_processL-phenylalanine catabolic process
B0009698biological_processphenylpropanoid metabolic process
B0009800biological_processcinnamic acid biosynthetic process
B0016597molecular_functionamino acid binding
B0016829molecular_functionlyase activity
B0016841molecular_functionammonia-lyase activity
B0032991cellular_componentprotein-containing complex
B0045548molecular_functionphenylalanine ammonia-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DTT A 1717
ChainResidue
APHE137
AMDO203
ALEU206
AASN260
AHOH2240
AHOH2386
AHOH2533
AHOH2534

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DTT B 1717
ChainResidue
BMDO203
BLEU206
BASN260
BHOH2392
BHOH2400
BHOH2537
BPHE137

Functional Information from PROSITE/UniProt
site_idPS00488
Number of Residues17
DetailsPAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GTITASGDLvPLSyiaG
ChainResidueDetails
AGLY198-LEU216

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q68G84","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q68G84","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P11544","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"2,3-didehydroalanine (Ser)","evidences":[{"source":"PubMed","id":"8050576","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsCross-link: {"description":"5-imidazolinone (Ala-Gly)","evidences":[{"source":"UniProtKB","id":"Q68G84","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 15548745
ChainResidueDetails
APHE400
BTYR351

site_idCSA2
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 15548745
ChainResidueDetails
BPHE400

site_idCSA3
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 15548745
ChainResidueDetails
APHE400
BTYR351

site_idCSA4
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 15548745
ChainResidueDetails
ATYR351

site_idMCSA1
Number of Residues3
DetailsM-CSA 708
ChainResidueDetails
ATYR110increase acidity, promote heterolysis, proton donor
ATHR355proton acceptor, proton donor, proton relay
APRO404electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 708
ChainResidueDetails
BTYR110increase acidity, promote heterolysis, proton donor
BTHR355proton acceptor, proton donor, proton relay
BPRO404electrostatic stabiliser

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PDB entries from 2025-12-24

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