2C44
Crystal Structure of E. coli Tryptophanase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
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 | tryptophan metabolic process |
A | 0006569 | biological_process | 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 | 0003824 | molecular_function | catalytic 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 | tryptophan metabolic process |
B | 0006569 | biological_process | 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 | 0003824 | molecular_function | catalytic 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 | tryptophan metabolic process |
C | 0006569 | biological_process | 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 | 0003824 | molecular_function | catalytic 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 | tryptophan metabolic process |
D | 0006569 | biological_process | 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 | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | LYS5 | |
C | LYS115 | |
C | LYS156 | |
C | LYS450 | |
D | LYS5 | |
D | LYS115 | |
D | LYS156 | |
D | LYS450 | |
A | LYS115 | |
A | LYS156 | |
A | LYS450 | |
B | LYS5 | |
B | LYS115 | |
B | LYS156 | |
B | LYS450 | |
C | LYS5 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LYS270 | |
B | LYS270 | |
C | LYS270 | |
D | LYS270 |
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 |