2O0T

The three dimensional structure of diaminopimelate decarboxylase from Mycobacterium tuberculosis reveals a tetrameric enzyme organisation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005515	molecular_function	protein binding
A	0008652	biological_process	amino acid biosynthetic process
A	0008836	molecular_function	diaminopimelate decarboxylase activity
A	0009085	biological_process	L-lysine biosynthetic process
A	0009089	biological_process	L-lysine biosynthetic process via diaminopimelate
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0030170	molecular_function	pyridoxal phosphate binding
B	0003824	molecular_function	catalytic activity
B	0005515	molecular_function	protein binding
B	0008652	biological_process	amino acid biosynthetic process
B	0008836	molecular_function	diaminopimelate decarboxylase activity
B	0009085	biological_process	L-lysine biosynthetic process
B	0009089	biological_process	L-lysine biosynthetic process via diaminopimelate
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0016829	molecular_function	lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0030170	molecular_function	pyridoxal phosphate binding
C	0003824	molecular_function	catalytic activity
C	0005515	molecular_function	protein binding
C	0008652	biological_process	amino acid biosynthetic process
C	0008836	molecular_function	diaminopimelate decarboxylase activity
C	0009085	biological_process	L-lysine biosynthetic process
C	0009089	biological_process	L-lysine biosynthetic process via diaminopimelate
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0016829	molecular_function	lyase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0030170	molecular_function	pyridoxal phosphate binding
D	0003824	molecular_function	catalytic activity
D	0005515	molecular_function	protein binding
D	0008652	biological_process	amino acid biosynthetic process
D	0008836	molecular_function	diaminopimelate decarboxylase activity
D	0009085	biological_process	L-lysine biosynthetic process
D	0009089	biological_process	L-lysine biosynthetic process via diaminopimelate
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0016829	molecular_function	lyase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 501

Chain	Residue
A	GLY258
A	GLY302
A	ARG303
A	TYR405
A	HOH503
A	HOH515
A	HOH573

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 502

Chain	Residue
B	ARG303
B	TYR405
B	HOH505
B	HOH508
B	HOH580
B	GLY258
B	GLY302

---

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. YAaKAFlcseVArwIseeG

Chain	Residue	Details
A	TYR69-GLY87

---

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

Chain	Residue	Details
A	GLY243-GLY260

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_02120","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12637582","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12637582","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02120","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12637582","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02120","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"12637582","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS182

---

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

Chain	Residue	Details
D	LYS182

---

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

Chain	Residue	Details
C	LYS182

---

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

Chain	Residue	Details
B	LYS182

---

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
A	GLU300
A	HIS213

---

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
B	GLU300
B	HIS213

---

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
C	GLU300
C	HIS213

---

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1bd0

Chain	Residue	Details
D	GLU300
D	HIS213

---