3N2B

1.8 Angstrom Resolution Crystal Structure of Diaminopimelate Decarboxylase (lysA) from Vibrio cholerae.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0008652	biological_process	amino acid biosynthetic process
A	0008836	molecular_function	diaminopimelate decarboxylase activity
A	0009085	biological_process	lysine biosynthetic process
A	0009089	biological_process	lysine biosynthetic process via diaminopimelate
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	0008652	biological_process	amino acid biosynthetic process
B	0008836	molecular_function	diaminopimelate decarboxylase activity
B	0009085	biological_process	lysine biosynthetic process
B	0009089	biological_process	lysine biosynthetic process via diaminopimelate
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	0008652	biological_process	amino acid biosynthetic process
C	0008836	molecular_function	diaminopimelate decarboxylase activity
C	0009085	biological_process	lysine biosynthetic process
C	0009089	biological_process	lysine biosynthetic process via diaminopimelate
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	0008652	biological_process	amino acid biosynthetic process
D	0008836	molecular_function	diaminopimelate decarboxylase activity
D	0009085	biological_process	lysine biosynthetic process
D	0009089	biological_process	lysine biosynthetic process via diaminopimelate
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	3
Details	BINDING SITE FOR RESIDUE CL A 418

Chain	Residue
A	GLU128
A	ARG178
B	LYS295

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 418

Chain	Residue
C	PRO276
C	GLY277
C	ARG278
C	ALA279
C	HOH992

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 419

Chain	Residue
C	PRO161
C	TYR162
C	ILE163
C	HOH619
C	HIS160

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL D 418

Chain	Residue
D	GLY240
D	PRO276
D	GLY277
D	ARG278
D	ALA279
D	HOH1079

---

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. YAvKANsnlgVLntLarlG

Chain	Residue	Details
A	TYR58-GLY76

---

site_id	PS00879
Number of Residues	16
Details	ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. Aegih..IrHLDVGGGLG

Chain	Residue	Details
A	ALA227-GLY242

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	32
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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