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	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	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	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	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	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	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	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	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	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"}

Chain

Residue

Details

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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	ARG462	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	ARG462	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	ARG462	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	ARG462	activator, electrostatic stabiliser

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