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4UP2

Crystal structure of Escherichia coli tryptophanase purified from alkaline stressed bacterial culture.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0006568biological_processL-tryptophan metabolic process
A0006569biological_processL-tryptophan 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
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0006568biological_processL-tryptophan metabolic process
B0006569biological_processL-tryptophan 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
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006520biological_processamino acid metabolic process
C0006568biological_processL-tryptophan metabolic process
C0006569biological_processL-tryptophan catabolic process
C0009034molecular_functiontryptophanase activity
C0009072biological_processaromatic amino acid metabolic process
C0016020cellular_componentmembrane
C0016829molecular_functionlyase activity
C0016830molecular_functioncarbon-carbon lyase activity
C0030170molecular_functionpyridoxal phosphate binding
C0030955molecular_functionpotassium ion binding
C0032991cellular_componentprotein-containing complex
C0042431biological_processindole metabolic process
C0042802molecular_functionidentical protein binding
C0060187cellular_componentcell pole
C0080146molecular_functionL-cysteine desulfhydrase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006520biological_processamino acid metabolic process
D0006568biological_processL-tryptophan metabolic process
D0006569biological_processL-tryptophan catabolic process
D0009034molecular_functiontryptophanase activity
D0009072biological_processaromatic amino acid metabolic process
D0016020cellular_componentmembrane
D0016829molecular_functionlyase activity
D0016830molecular_functioncarbon-carbon lyase activity
D0030170molecular_functionpyridoxal phosphate binding
D0030955molecular_functionpotassium ion binding
D0032991cellular_componentprotein-containing complex
D0042431biological_processindole metabolic process
D0042802molecular_functionidentical protein binding
D0060187cellular_componentcell pole
D0080146molecular_functionL-cysteine desulfhydrase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1469
ChainResidue
ASER54
AGLN101
AGLY102
AARG103
ASER267
ALYS269

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1470
ChainResidue
BGLY55
BPRO275
AGLU72
ALEU310
BSER54

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1471
ChainResidue
AVAL388
AALA389
APHE434
AGLU437
AALA438

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 1455
ChainResidue
AMET1
CVAL388
CALA389
CPHE434
CGLU437
CALA438

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1472
ChainResidue
ATHR23
AARG24

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1473
ChainResidue
AALA84
AGLN94
AHOH2018
AHOH2039

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1474
ChainResidue
ATHR52
AASP53
ALYS270
AARG419

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1454
ChainResidue
AGLY55
APRO275
BGLU72
BLEU310

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1455
ChainResidue
BTRP248
BGLN252
BHOH2029

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1456
ChainResidue
BTYR74
BTYR307

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1457
ChainResidue
BTYR307
BHOH2030
BHOH2031

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1458
ChainResidue
BGLY102
BARG103
BSER267
BLYS269

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 1455
ChainResidue
BGLU2
DVAL388
DALA389
DPHE434
DGLU437
DALA438

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1459
ChainResidue
BTHR60
BSER62
BASP324
BHOH2023
DPRO18

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1460
ChainResidue
BTHR22
BTHR23
BARG24
BARG27

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME B 1461
ChainResidue
BSER75
BGLY76

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 1456
ChainResidue
CGLN101
CGLY102
CARG103
CSER267
CLYS269

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 1457
ChainResidue
CTHR52
CLYS270

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 1458
ChainResidue
CTHR22
CTHR23
CARG24
CARG27
CHOH2004
CHOH2024

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 1456
ChainResidue
CGLU72
DSER54
DGLY55
DLYS269
DPRO275

site_idCC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 1459
ChainResidue
CGLN94
CHOH2011

site_idCC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 C 1460
ChainResidue
CSER398

site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 1461
ChainResidue
BLYS211
CLYS211
CGLU244
CTYR245
CGLU256

site_idCC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 C 1462
ChainResidue
CPRO414

site_idCC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 1457
ChainResidue
CSER54
CGLY55
DGLU72
DALA73

site_idCC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 1458
ChainResidue
DSER267
DLYS269
DGLN101
DGLY102
DARG103

site_idCC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 D 1459
ChainResidue
CGLN101
DLEU310

site_idDC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 D 1460
ChainResidue
DLEU452
DTHR453

site_idDC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1462
ChainResidue
BVAL388
BPHE434
BGLU437
BALA438
DGLU2

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

246905

PDB entries from 2025-12-31

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