2I5B

The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parralel emergence of enzyme activity during evolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0008478	molecular_function	pyridoxal kinase activity
A	0008902	molecular_function	hydroxymethylpyrimidine kinase activity
A	0008972	molecular_function	phosphomethylpyrimidine kinase activity
A	0009228	biological_process	thiamine biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0008478	molecular_function	pyridoxal kinase activity
B	0008902	molecular_function	hydroxymethylpyrimidine kinase activity
B	0008972	molecular_function	phosphomethylpyrimidine kinase activity
B	0009228	biological_process	thiamine biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0008478	molecular_function	pyridoxal kinase activity
C	0008902	molecular_function	hydroxymethylpyrimidine kinase activity
C	0008972	molecular_function	phosphomethylpyrimidine kinase activity
C	0009228	biological_process	thiamine biosynthetic process
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0005829	cellular_component	cytosol
D	0008478	molecular_function	pyridoxal kinase activity
D	0008902	molecular_function	hydroxymethylpyrimidine kinase activity
D	0008972	molecular_function	phosphomethylpyrimidine kinase activity
D	0009228	biological_process	thiamine biosynthetic process
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0005524	molecular_function	ATP binding
E	0005829	cellular_component	cytosol
E	0008478	molecular_function	pyridoxal kinase activity
E	0008902	molecular_function	hydroxymethylpyrimidine kinase activity
E	0008972	molecular_function	phosphomethylpyrimidine kinase activity
E	0009228	biological_process	thiamine biosynthetic process
E	0016301	molecular_function	kinase activity
E	0016740	molecular_function	transferase activity
E	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADP A 301

Chain	Residue
A	ASN141
A	ALA214
A	GLY215
A	LYS240
A	ILE243
A	ILE247
A	THR178
A	GLY180
A	GLY181
A	LYS182
A	ALA188
A	ASP190
A	GLU204
A	ILE206

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADP C 401

Chain	Residue
C	ASN141
C	THR178
C	GLY180
C	GLY181
C	LYS182
C	ALA188
C	ASP190
C	GLU204
C	ILE206
C	ALA214
C	GLY215
C	LYS240
C	ILE243
C	ILE247

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADP D 501

Chain	Residue
D	ASN141
D	THR178
D	GLY180
D	GLY181
D	LYS182
D	ALA188
D	ASP190
D	GLU204
D	ILE206
D	ALA214
D	GLY215
D	LYS240
D	ILE243
D	ILE247

---

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADP B 601

Chain	Residue
B	ASN141
B	THR178
B	GLY180
B	GLY181
B	LYS182
B	ALA188
B	ASP190
B	GLU204
B	ILE206
B	ALA214
B	GLY215
B	LYS240
B	ILE243
B	ILE247

---

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADP E 701

Chain	Residue
E	ASN141
E	THR178
E	GLY180
E	GLY181
E	LYS182
E	ALA188
E	ASP190
E	GLU204
E	ILE206
E	ALA214
E	GLY215
E	LYS240
E	ILE243
E	ILE247

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	45
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1tz3

Chain	Residue	Details
A	GLY215
A	CYS216
A	GLY213
A	ALA214

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1tz3

Chain	Residue	Details
C	GLY215
C	CYS216
C	GLY213
C	ALA214

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1tz3

Chain	Residue	Details
D	GLY215
D	CYS216
D	GLY213
D	ALA214

---

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1tz3

Chain	Residue	Details
B	GLY215
B	CYS216
B	GLY213
B	ALA214

---

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1tz3

Chain	Residue	Details
E	GLY215
E	CYS216
E	GLY213
E	ALA214

---