Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1T6J

Crystal Structure of Phenylalanine Ammonia Lyase from Rhodosporidium 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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CIN B 1001
ChainResidue
B175211
BLEU266
BASN397
BLYS468
BGLU496
BGLN500

Functional Information from PROSITE/UniProt
site_idPS00488
Number of Residues17
DetailsPAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GTISASGDLsPLSyiaA
ChainResidueDetails
AGLY207-ILE225

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q68G84
ChainResidueDetails
ATYR110
BTYR110

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q68G84
ChainResidueDetails
ATHR272
BALA501
AARG362
ASER368
ALEU399
AALA501
BTHR272
BARG362
BSER368
BLEU399

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15350127, ECO:0007744|PDB:1T6J
ChainResidueDetails
ALEU470
AALA498
BLEU470
BALA498

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: 2,3-didehydroalanine (Ser) => ECO:0000269|PubMed:15350127
ChainResidueDetails
AASP214
BASP214

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: 5-imidazolinone (Ala-Gly) => ECO:0000269|PubMed:15350127
ChainResidueDetails
A175211
ALEU215
B175211
BLEU215

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon