1AX4
TRYPTOPHANASE FROM PROTEUS VULGARIS
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0016829 | molecular_function | lyase activity |
A | 0016830 | molecular_function | carbon-carbon lyase activity |
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 | 0016829 | molecular_function | lyase activity |
B | 0016830 | molecular_function | carbon-carbon lyase activity |
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 | 0016829 | molecular_function | lyase activity |
C | 0016830 | molecular_function | carbon-carbon lyase activity |
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 | 0016829 | molecular_function | lyase activity |
D | 0016830 | molecular_function | carbon-carbon lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 500 |
Chain | Residue |
A | GLY53 |
A | ASN271 |
A | HOH544 |
B | GLU70 |
B | HOH515 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K B 500 |
Chain | Residue |
A | GLU70 |
A | HOH521 |
B | GLY53 |
B | ASN271 |
B | HOH503 |
B | HOH513 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K C 500 |
Chain | Residue |
C | GLY53 |
C | ASN271 |
C | HOH506 |
C | HOH529 |
D | GLU70 |
D | HOH509 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K D 500 |
Chain | Residue |
C | GLU70 |
C | HOH511 |
C | HOH512 |
D | GLY53 |
D | ASN271 |
D | HOH517 |
site_id | LPA |
Number of Residues | 14 |
Details | PYRIDOXAL 5'-PHOSPHATE BINDING SITE. |
Chain | Residue |
A | LLP266 |
A | ARG226 |
A | MET222 |
A | ASN194 |
A | PHE132 |
A | ALA225 |
A | GLY100 |
A | ARG101 |
A | GLN99 |
A | SER263 |
A | SER52 |
A | LYS265 |
B | TYR72 |
B | TYR301 |
site_id | LPB |
Number of Residues | 14 |
Details | PYRIDOXAL 5'-PHOSPHATE BINDING SITE. |
Chain | Residue |
B | LLP266 |
B | ARG226 |
B | MET222 |
B | ASN194 |
B | PHE132 |
B | ALA225 |
B | GLY100 |
B | ARG101 |
B | GLN99 |
B | SER263 |
B | SER52 |
B | LYS265 |
A | TYR72 |
A | TYR301 |
site_id | LPC |
Number of Residues | 14 |
Details | PYRIDOXAL 5'-PHOSPHATE BINDING SITE. |
Chain | Residue |
C | LLP266 |
C | ARG226 |
C | MET222 |
C | ASN194 |
C | PHE132 |
C | ALA225 |
C | GLY100 |
C | ARG101 |
C | GLN99 |
C | SER263 |
C | SER52 |
C | LYS265 |
D | TYR72 |
D | TYR301 |
site_id | LPD |
Number of Residues | 14 |
Details | PYRIDOXAL 5'-PHOSPHATE BINDING SITE. |
Chain | Residue |
D | LLP266 |
D | ARG226 |
D | MET222 |
D | ASN194 |
D | PHE132 |
D | ALA225 |
D | GLY100 |
D | ARG101 |
D | GLN99 |
D | SER263 |
D | SER52 |
D | LYS265 |
C | TYR72 |
C | TYR301 |
site_id | POA |
Number of Residues | 3 |
Details | POTASSIUM BINDING SITE. |
Chain | Residue |
A | GLU70 |
B | GLY53 |
B | ASN271 |
site_id | POB |
Number of Residues | 3 |
Details | POTASSIUM BINDING SITE. |
Chain | Residue |
B | GLU70 |
A | GLY53 |
A | ASN271 |
site_id | POC |
Number of Residues | 3 |
Details | POTASSIUM BINDING SITE. |
Chain | Residue |
C | GLU70 |
D | GLY53 |
D | ASN271 |
site_id | POD |
Number of Residues | 3 |
Details | POTASSIUM BINDING SITE. |
Chain | Residue |
D | GLU70 |
C | GLY53 |
C | ASN271 |
Functional Information from PROSITE/UniProt
site_id | PS00853 |
Number of Residues | 19 |
Details | BETA_ELIM_LYASE Beta-eliminating lyases pyridoxal-phosphate attachment site. YaDaltMSAKKDpLLnIGG |
Chain | Residue | Details |
A | TYR256-GLY274 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LLP266 | |
B | LLP266 | |
C | LLP266 | |
D | LLP266 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | a catalytic site defined by CSA, PubMed 16455316, 9551100, 19425498 |
Chain | Residue | Details |
A | TYR72 | |
A | ASP133 | |
A | HIS458 |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 410 |
Chain | Residue | Details |
A | TYR72 | proton shuttle (general acid/base) |
A | PHE132 | steric role |
A | ASP133 | electrostatic stabiliser, proton shuttle (general acid/base) |
A | ASP223 | electrostatic stabiliser |
A | ALA225 | steric role |
A | LLP266 | covalent catalysis, proton shuttle (general acid/base) |
A | HIS458 | activator, electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 410 |
Chain | Residue | Details |
B | TYR72 | proton shuttle (general acid/base) |
B | PHE132 | steric role |
B | ASP133 | electrostatic stabiliser, proton shuttle (general acid/base) |
B | ASP223 | electrostatic stabiliser |
B | ALA225 | steric role |
B | LLP266 | covalent catalysis, proton shuttle (general acid/base) |
B | HIS458 | activator, electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 7 |
Details | M-CSA 410 |
Chain | Residue | Details |
C | TYR72 | proton shuttle (general acid/base) |
C | PHE132 | steric role |
C | ASP133 | electrostatic stabiliser, proton shuttle (general acid/base) |
C | ASP223 | electrostatic stabiliser |
C | ALA225 | steric role |
C | LLP266 | covalent catalysis, proton shuttle (general acid/base) |
C | HIS458 | activator, electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 7 |
Details | M-CSA 410 |
Chain | Residue | Details |
D | TYR72 | proton shuttle (general acid/base) |
D | PHE132 | steric role |
D | ASP133 | electrostatic stabiliser, proton shuttle (general acid/base) |
D | ASP223 | electrostatic stabiliser |
D | ALA225 | steric role |
D | LLP266 | covalent catalysis, proton shuttle (general acid/base) |
D | HIS458 | activator, electrostatic stabiliser |