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3CZO

Crystal Structure of Double Mutant Phenylalanine Ammonia-Lyase From Anabaena Variabilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004397molecular_functionhistidine ammonia-lyase activity
A0005737cellular_componentcytoplasm
A0009072biological_processaromatic amino acid metabolic process
A0009699biological_processphenylpropanoid biosynthetic process
A0009800biological_processcinnamic acid biosynthetic process
A0016841molecular_functionammonia-lyase activity
A0045548molecular_functionphenylalanine ammonia-lyase activity
A0051289biological_processprotein homotetramerization
B0003824molecular_functioncatalytic activity
B0004397molecular_functionhistidine ammonia-lyase activity
B0005737cellular_componentcytoplasm
B0009072biological_processaromatic amino acid metabolic process
B0009699biological_processphenylpropanoid biosynthetic process
B0009800biological_processcinnamic acid biosynthetic process
B0016841molecular_functionammonia-lyase activity
B0045548molecular_functionphenylalanine ammonia-lyase activity
B0051289biological_processprotein homotetramerization
C0003824molecular_functioncatalytic activity
C0004397molecular_functionhistidine ammonia-lyase activity
C0005737cellular_componentcytoplasm
C0009072biological_processaromatic amino acid metabolic process
C0009699biological_processphenylpropanoid biosynthetic process
C0009800biological_processcinnamic acid biosynthetic process
C0016841molecular_functionammonia-lyase activity
C0045548molecular_functionphenylalanine ammonia-lyase activity
C0051289biological_processprotein homotetramerization
D0003824molecular_functioncatalytic activity
D0004397molecular_functionhistidine ammonia-lyase activity
D0005737cellular_componentcytoplasm
D0009072biological_processaromatic amino acid metabolic process
D0009699biological_processphenylpropanoid biosynthetic process
D0009800biological_processcinnamic acid biosynthetic process
D0016841molecular_functionammonia-lyase activity
D0045548molecular_functionphenylalanine ammonia-lyase activity
D0051289biological_processprotein homotetramerization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q68G84","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q68G84","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P11544","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"2,3-didehydroalanine (Ser)","evidences":[{"source":"PubMed","id":"17240984","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsCross-link: {"description":"5-imidazolinone (Ala-Gly)","evidences":[{"source":"PubMed","id":"17240984","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

253091

PDB entries from 2026-05-06

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