6EEW

Crystal structure of Catharanthus roseus tryptophan decarboxylase in complex with L-tryptophan

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004058	molecular_function	aromatic-L-amino-acid decarboxylase activity
A	0005737	cellular_component	cytoplasm
A	0006520	biological_process	amino acid metabolic process
A	0016829	molecular_function	lyase activity
A	0016830	molecular_function	carbon-carbon lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0036467	molecular_function	5-hydroxy-L-tryptophan decarboxylase activity
A	0036469	molecular_function	L-tryptophan decarboxylase activity
B	0004058	molecular_function	aromatic-L-amino-acid decarboxylase activity
B	0005737	cellular_component	cytoplasm
B	0006520	biological_process	amino acid metabolic process
B	0016829	molecular_function	lyase activity
B	0016830	molecular_function	carbon-carbon lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0036467	molecular_function	5-hydroxy-L-tryptophan decarboxylase activity
B	0036469	molecular_function	L-tryptophan decarboxylase activity
C	0004058	molecular_function	aromatic-L-amino-acid decarboxylase activity
C	0005737	cellular_component	cytoplasm
C	0006520	biological_process	amino acid metabolic process
C	0016829	molecular_function	lyase activity
C	0016830	molecular_function	carbon-carbon lyase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0036467	molecular_function	5-hydroxy-L-tryptophan decarboxylase activity
C	0036469	molecular_function	L-tryptophan decarboxylase activity
D	0004058	molecular_function	aromatic-L-amino-acid decarboxylase activity
D	0005737	cellular_component	cytoplasm
D	0006520	biological_process	amino acid metabolic process
D	0016829	molecular_function	lyase activity
D	0016830	molecular_function	carbon-carbon lyase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	0036467	molecular_function	5-hydroxy-L-tryptophan decarboxylase activity
D	0036469	molecular_function	L-tryptophan decarboxylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue TRP A 601

Chain	Residue
A	PHE100
A	PHE101
A	THR262
A	LLP319

---

site_id	AC2
Number of Residues	3
Details	binding site for residue CA A 602

Chain	Residue
A	ASP397
A	HOH716
A	HOH728

---

site_id	AC3
Number of Residues	5
Details	binding site for residue TRP B 601

Chain	Residue
B	PHE101
B	HIS318
B	LLP319
A	PHE124
B	TRP92

---

site_id	AC4
Number of Residues	4
Details	binding site for residue CA B 602

Chain	Residue
B	ASP397
B	HOH709
B	HOH745
B	HOH749

---

site_id	AC5
Number of Residues	7
Details	binding site for residue TRP C 601

Chain	Residue
C	TRP92
C	PHE101
C	HIS203
C	THR262
C	HIS318
C	LLP319
D	THR369

---

site_id	AC6
Number of Residues	3
Details	binding site for residue CA C 602

Chain	Residue
C	ASP397
C	HOH715
C	HOH738

---

site_id	AC7
Number of Residues	5
Details	binding site for residue TRP D 601

Chain	Residue
C	VAL122
C	PHE124
C	THR369
D	HIS318
D	LLP319

---

site_id	AC8
Number of Residues	1
Details	binding site for residue CA D 602

Chain	Residue
D	ASP397

---

Functional Information from PROSITE/UniProt

site_id	PS00392
Number of Residues	22
Details	DDC_GAD_HDC_YDC DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site. SLsLsphKWLlAyLDCtcLWvK

Chain	Residue	Details
A	SER312-LYS333

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	13
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32371491","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6EEW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"32371491","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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