2C44
Crystal Structure of E. coli Tryptophanase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006568 | biological_process | L-tryptophan metabolic process |
| A | 0006569 | biological_process | L-tryptophan catabolic process |
| A | 0009034 | molecular_function | tryptophanase activity |
| A | 0009072 | biological_process | aromatic amino acid metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042431 | biological_process | indole metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0060187 | cellular_component | cell pole |
| A | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006568 | biological_process | L-tryptophan metabolic process |
| B | 0006569 | biological_process | L-tryptophan catabolic process |
| B | 0009034 | molecular_function | tryptophanase activity |
| B | 0009072 | biological_process | aromatic amino acid metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0030955 | molecular_function | potassium ion binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042431 | biological_process | indole metabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0060187 | cellular_component | cell pole |
| B | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006568 | biological_process | L-tryptophan metabolic process |
| C | 0006569 | biological_process | L-tryptophan catabolic process |
| C | 0009034 | molecular_function | tryptophanase activity |
| C | 0009072 | biological_process | aromatic amino acid metabolic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016830 | molecular_function | carbon-carbon lyase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0030955 | molecular_function | potassium ion binding |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0042431 | biological_process | indole metabolic process |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0060187 | cellular_component | cell pole |
| C | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006568 | biological_process | L-tryptophan metabolic process |
| D | 0006569 | biological_process | L-tryptophan catabolic process |
| D | 0009034 | molecular_function | tryptophanase activity |
| D | 0009072 | biological_process | aromatic amino acid metabolic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016830 | molecular_function | carbon-carbon lyase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0030955 | molecular_function | potassium ion binding |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0042431 | biological_process | indole metabolic process |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0060187 | cellular_component | cell pole |
| D | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 500 |
| Chain | Residue |
| A | GLN101 |
| A | GLY102 |
| A | ARG103 |
| A | SER267 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | THR52 |
| A | ASN198 |
| A | ARG230 |
| A | LYS270 |
| A | ARG419 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A1471 |
| Chain | Residue |
| A | GLY55 |
| A | PRO275 |
| A | HOH2084 |
| B | GLU72 |
| B | HOH2091 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A1472 |
| Chain | Residue |
| A | GLN107 |
| A | GLN301 |
| A | GLU302 |
| B | GLN107 |
| B | GLN301 |
| B | GLU302 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 500 |
| Chain | Residue |
| B | GLN101 |
| B | GLY102 |
| B | ARG103 |
| B | SER267 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 501 |
| Chain | Residue |
| B | THR52 |
| B | ASN198 |
| B | ARG230 |
| B | LYS270 |
| B | ARG419 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K B1472 |
| Chain | Residue |
| A | GLU72 |
| B | GLY55 |
| B | PRO275 |
| B | HOH2028 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 500 |
| Chain | Residue |
| C | GLN101 |
| C | GLY102 |
| C | ARG103 |
| C | SER267 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 501 |
| Chain | Residue |
| C | THR52 |
| C | ASN198 |
| C | ARG230 |
| C | LYS270 |
| C | ARG419 |
| C | HOH2125 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K C1472 |
| Chain | Residue |
| C | GLY55 |
| C | PRO275 |
| D | GLU72 |
| D | HOH2090 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C1473 |
| Chain | Residue |
| C | GLN107 |
| C | GLN301 |
| C | GLU302 |
| D | GLN107 |
| D | GLN301 |
| D | GLU302 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 500 |
| Chain | Residue |
| D | GLN101 |
| D | GLY102 |
| D | ARG103 |
| D | SER267 |
| D | LYS270 |
| D | HOH2120 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 501 |
| Chain | Residue |
| D | THR52 |
| D | ASN198 |
| D | ARG230 |
| D | LYS270 |
| D | ARG419 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K D1471 |
| Chain | Residue |
| C | GLU72 |
| C | HOH2033 |
| D | GLY55 |
| D | PRO275 |
Functional Information from PROSITE/UniProt
| site_id | PS00853 |
| Number of Residues | 19 |
| Details | BETA_ELIM_LYASE Beta-eliminating lyases pyridoxal-phosphate attachment site. YaDmlaMSAKKDaMVpMGG |
| Chain | Residue | Details |
| A | TYR260-GLY278 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | PHE135 | |
| A | ASP227 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | PHE135 | |
| B | LYS270 | |
| B | ASP227 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | PHE135 | |
| C | LYS270 | |
| C | ASP227 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | PHE135 | |
| D | LYS270 | |
| D | ASP227 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | PHE136 | |
| A | LYS270 | |
| A | ASP227 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | PHE136 | |
| B | LYS270 | |
| B | ASP227 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | PHE136 | |
| C | LYS270 | |
| C | ASP227 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | PHE136 | |
| D | LYS270 | |
| D | ASP227 |
| site_id | CSA17 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | PHE136 | |
| A | LYS259 | |
| A | ASP227 |
| site_id | CSA18 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | PHE136 | |
| B | LYS259 | |
| B | ASP227 |
| site_id | CSA19 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | PHE136 | |
| C | LYS259 | |
| C | ASP227 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | PHE135 | |
| D | ASP227 |
| site_id | CSA20 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | PHE136 | |
| D | LYS259 | |
| D | ASP227 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | PHE135 | |
| C | ASP227 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | PHE135 | |
| B | ASP227 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | PHE136 | |
| A | ASP227 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | PHE136 | |
| B | ASP227 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | PHE136 | |
| C | ASP227 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | PHE136 | |
| D | ASP227 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | PHE135 | |
| A | LYS270 | |
| A | ASP227 |
