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5D8G

A structural view on the dissociation of E. coli Tryptophanase

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 Residues2
Detailsbinding site for residue CL A 1001
ChainResidue
AARG69
AARG69

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 1002
ChainResidue
AHOH1156
AHOH1180
AHOH1213
AHOH1235
AHOH1419
AHOH1448

site_idAC3
Number of Residues7
Detailsbinding site for residue EPE A 1003
ChainResidue
ATHR52
ATYR74
ATYR307
ALEU400
AARG419
AHOH1177
ALEU51

site_idAC4
Number of Residues4
Detailsbinding site for residue MG A 1004
ChainResidue
AGLN119
AGLU293
AHOH1111
AHOH1125

site_idAC5
Number of Residues6
Detailsbinding site for residue MG A 1005
ChainResidue
AASP53
AARG334
AHIS358
ATHR421
AILE422
AHOH1383

site_idAC6
Number of Residues3
Detailsbinding site for residue NA A 1006
ChainResidue
AGLU251
AHOH1185
AHOH1234

site_idAC7
Number of Residues4
Detailsbinding site for residue CA A 1007
ChainResidue
AARG69
AGLU316
AVAL320
AHOH1498

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

224931

PDB entries from 2024-09-11

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