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

2V0Y

Crystal structure of apo C298S tryptophanase from E.coli

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 1472
ChainResidue
AALA65
AALA65
AARG69
AARG69
AHOH2116
AHOH2116

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1474
ChainResidue
AHOH2350
AHOH2376
AHOH2105
AHOH2131
AHOH2132

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS5
ALYS115
ALYS156
ALYS450

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS270

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
APHE136
AASP227

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
APHE135
ALYS270
AASP227

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
APHE136
ALYS270
AASP227

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
APHE136
ALYS259
AASP227

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
APHE135
AASP227

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon