1QU4

CRYSTAL STRUCTURE OF TRYPANOSOMA BRUCEI ORNITHINE DECARBOXYLASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004586	molecular_function	ornithine decarboxylase activity
A	0005737	cellular_component	cytoplasm
A	0006595	biological_process	polyamine metabolic process
A	0006596	biological_process	polyamine biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0033387	biological_process	putrescine biosynthetic process from arginine, via ornithine
B	0003824	molecular_function	catalytic activity
B	0004586	molecular_function	ornithine decarboxylase activity
B	0005737	cellular_component	cytoplasm
B	0006595	biological_process	polyamine metabolic process
B	0006596	biological_process	polyamine biosynthetic process
B	0016829	molecular_function	lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0033387	biological_process	putrescine biosynthetic process from arginine, via ornithine
C	0003824	molecular_function	catalytic activity
C	0004586	molecular_function	ornithine decarboxylase activity
C	0005737	cellular_component	cytoplasm
C	0006595	biological_process	polyamine metabolic process
C	0006596	biological_process	polyamine biosynthetic process
C	0016829	molecular_function	lyase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0033387	biological_process	putrescine biosynthetic process from arginine, via ornithine
D	0003824	molecular_function	catalytic activity
D	0004586	molecular_function	ornithine decarboxylase activity
D	0005737	cellular_component	cytoplasm
D	0006595	biological_process	polyamine metabolic process
D	0006596	biological_process	polyamine biosynthetic process
D	0016829	molecular_function	lyase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0033387	biological_process	putrescine biosynthetic process from arginine, via ornithine

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP A 600

Chain	Residue
A	ALA67
A	GLY276
A	ARG277
A	TYR389
B	CYS360
A	LYS69
A	ASP88
A	ARG154
A	HIS197
A	SER200
A	GLY236
A	GLY237
A	GLU274

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP B 600

Chain	Residue
A	CYS360
B	ALA67
B	LYS69
B	ASP88
B	ARG154
B	HIS197
B	SER200
B	GLY236
B	GLY237
B	GLU274
B	GLY276
B	ARG277
B	TYR389

---

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP C 600

Chain	Residue
C	LYS69
C	ASP88
C	ARG154
C	HIS197
C	SER200
C	GLY236
C	GLY237
C	GLU274
C	GLY276
C	ARG277
C	TYR389
D	CYS360

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP D 600

Chain	Residue
C	CYS360
D	LYS69
D	ASP88
D	ARG154
D	HIS197
D	SER200
D	GLY236
D	GLY237
D	GLU274
D	GLY276
D	ARG277
D	TYR389

---

Functional Information from PROSITE/UniProt

site_id	PS00878
Number of Residues	19
Details	ODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YAvKCNddwrVLgtLaalG

Chain	Residue	Details
A	TYR66-GLY84

---

site_id	PS00879
Number of Residues	18
Details	ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. GtelgfnMhILDIGGGFP

Chain	Residue	Details
A	GLY222-PRO239

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor; shared with dimeric partner","evidences":[{"source":"PubMed","id":"10985770","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15476392","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10563800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10985770","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15476392","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"10563800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10985770","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10563800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10985770","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates","evidences":[{"source":"PubMed","id":"10563800","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10563800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15476392","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QU4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
A	LYS169
A	LYS69

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
B	LYS169
B	LYS69

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
C	LYS169
C	LYS69

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
D	LYS169
D	LYS69

---

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
A	GLU274
A	LYS69
A	HIS197

---

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
B	GLU274
B	LYS69
B	HIS197

---

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
C	GLU274
C	LYS69
C	HIS197

---

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
D	GLU274
D	LYS69
D	HIS197

---