1IXP

Enzyme-phosphate Complex of Pyridoxine 5'-Phosphate synthase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008615	biological_process	pyridoxine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016769	molecular_function	transferase activity, transferring nitrogenous groups
A	0033856	molecular_function	pyridoxine 5'-phosphate synthase activity
A	0042802	molecular_function	identical protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008615	biological_process	pyridoxine biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016769	molecular_function	transferase activity, transferring nitrogenous groups
B	0033856	molecular_function	pyridoxine 5'-phosphate synthase activity
B	0042802	molecular_function	identical protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008615	biological_process	pyridoxine biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016769	molecular_function	transferase activity, transferring nitrogenous groups
C	0033856	molecular_function	pyridoxine 5'-phosphate synthase activity
C	0042802	molecular_function	identical protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0008615	biological_process	pyridoxine biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016769	molecular_function	transferase activity, transferring nitrogenous groups
D	0033856	molecular_function	pyridoxine 5'-phosphate synthase activity
D	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 1001

Chain	Residue
A	ASP11
A	HIS12
A	ARG20
A	HIS52
A	HOH1087
A	HOH1089

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 1002

Chain	Residue
A	GLY194
A	ILE214
A	GLY215
A	HIS216
A	HOH1034
A	HOH1087
A	ARG20
A	GLY192
A	HIS193

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 C 1003

Chain	Residue
B	ARG20
C	GLY192
C	HIS193
C	GLY194
C	ASN213
C	ILE214
C	GLY215
C	HIS216
C	ALA217
C	HOH1100

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 C 1004

Chain	Residue
B	ARG20
C	ASP11
C	HIS12
C	HIS45
C	HIS52
C	HOH1100

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 B 1005

Chain	Residue
B	GLY192
B	HIS193
B	GLY194
B	ILE214
B	GLY215
B	HIS216
B	HOH1091
C	ARG20

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 B 1006

Chain	Residue
B	ASP11
B	HIS12
B	HIS45
B	HIS52
C	ARG20
C	HOH1065

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 D 1007

Chain	Residue
D	ASP11
D	HIS12
D	ARG20
D	HIS45
D	HIS52
D	HOH1012
D	HOH1123

---

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 D 1008

Chain	Residue
D	ARG20
D	GLY192
D	HIS193
D	GLY194
D	ASN213
D	ILE214
D	GLY215
D	HIS216
D	ALA217
D	HOH1012
D	HOH1114

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	32
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 243

Chain	Residue	Details
A	ASN9	electrostatic stabiliser, hydrogen bond donor
A	HIS12	attractive charge-charge interaction, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS45	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ARG47	attractive charge-charge interaction, electrostatic stabiliser, increase acidity, increase basicity
A	ARG51	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity
A	GLU72	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	THR103	electrostatic stabiliser, hydrogen bond acceptor
A	GLU153	electrostatic stabiliser, hydrogen bond acceptor
A	HIS193	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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site_id	MCSA2
Number of Residues	9
Details	M-CSA 243

Chain	Residue	Details
B	ASN9	electrostatic stabiliser, hydrogen bond donor
B	HIS12	attractive charge-charge interaction, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS45	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ARG47	attractive charge-charge interaction, electrostatic stabiliser, increase acidity, increase basicity
B	ARG51	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity
B	GLU72	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	THR103	electrostatic stabiliser, hydrogen bond acceptor
B	GLU153	electrostatic stabiliser, hydrogen bond acceptor
B	HIS193	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

---

site_id	MCSA3
Number of Residues	9
Details	M-CSA 243

Chain	Residue	Details
C	ASN9	electrostatic stabiliser, hydrogen bond donor
C	HIS12	attractive charge-charge interaction, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	HIS45	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ARG47	attractive charge-charge interaction, electrostatic stabiliser, increase acidity, increase basicity
C	ARG51	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity
C	GLU72	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	THR103	electrostatic stabiliser, hydrogen bond acceptor
C	GLU153	electrostatic stabiliser, hydrogen bond acceptor
C	HIS193	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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site_id	MCSA4
Number of Residues	9
Details	M-CSA 243

Chain	Residue	Details
D	ASN9	electrostatic stabiliser, hydrogen bond donor
D	HIS12	attractive charge-charge interaction, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	HIS45	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ARG47	attractive charge-charge interaction, electrostatic stabiliser, increase acidity, increase basicity
D	ARG51	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity
D	GLU72	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	THR103	electrostatic stabiliser, hydrogen bond acceptor
D	GLU153	electrostatic stabiliser, hydrogen bond acceptor
D	HIS193	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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