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

4W1Y

Crystal structure of Escherichia coli Tryptophanase in 'semi-holo' form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0006568biological_processtryptophan metabolic process
A0006569biological_processtryptophan catabolic process
A0009034molecular_functiontryptophanase activity
A0009072biological_processaromatic amino acid metabolic process
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0016830molecular_functioncarbon-carbon lyase activity
A0030170molecular_functionpyridoxal phosphate binding
A0030955molecular_functionpotassium ion binding
A0032991cellular_componentprotein-containing complex
A0042431biological_processindole metabolic process
A0042802molecular_functionidentical protein binding
A0060187cellular_componentcell pole
A0080146molecular_functionL-cysteine desulfhydrase activity
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0006568biological_processtryptophan metabolic process
B0006569biological_processtryptophan catabolic process
B0009034molecular_functiontryptophanase activity
B0009072biological_processaromatic amino acid metabolic process
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0016830molecular_functioncarbon-carbon lyase activity
B0030170molecular_functionpyridoxal phosphate binding
B0030955molecular_functionpotassium ion binding
B0032991cellular_componentprotein-containing complex
B0042431biological_processindole metabolic process
B0042802molecular_functionidentical protein binding
B0060187cellular_componentcell pole
B0080146molecular_functionL-cysteine desulfhydrase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 B 500
ChainResidue
BSER54
BGLN101
BGLY102
BARG103
BSER267
BLYS269

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 B 501
ChainResidue
BLYS270
BHOH602
BHOH631
BTHR52
BASP53
BARG230

Functional Information from PROSITE/UniProt
site_idPS00853
Number of Residues19
DetailsBETA_ELIM_LYASE Beta-eliminating lyases pyridoxal-phosphate attachment site. YaDmlaMSAKKDaMVpMGG
ChainResidueDetails
BTYR260-GLY278
ATYR260-GLY278

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
BLYS5
BLYS115
BLYS156
BLYS450

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
BLYS270

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon