5LNT

Crystal structure of Arabidopsis thaliana Pdx1K166R-preI320 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0008615	biological_process	pyridoxine biosynthetic process
A	0009507	cellular_component	chloroplast
A	0016829	molecular_function	lyase activity
A	0016843	molecular_function	amine-lyase activity
A	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
A	0042819	biological_process	vitamin B6 biosynthetic process
A	0042823	biological_process	pyridoxal phosphate biosynthetic process
A	0046982	molecular_function	protein heterodimerization activity
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005829	cellular_component	cytosol
B	0006520	biological_process	amino acid metabolic process
B	0008615	biological_process	pyridoxine biosynthetic process
B	0009507	cellular_component	chloroplast
B	0016829	molecular_function	lyase activity
B	0016843	molecular_function	amine-lyase activity
B	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
B	0042819	biological_process	vitamin B6 biosynthetic process
B	0042823	biological_process	pyridoxal phosphate biosynthetic process
B	0046982	molecular_function	protein heterodimerization activity
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0005829	cellular_component	cytosol
C	0006520	biological_process	amino acid metabolic process
C	0008615	biological_process	pyridoxine biosynthetic process
C	0009507	cellular_component	chloroplast
C	0016829	molecular_function	lyase activity
C	0016843	molecular_function	amine-lyase activity
C	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
C	0042819	biological_process	vitamin B6 biosynthetic process
C	0042823	biological_process	pyridoxal phosphate biosynthetic process
C	0046982	molecular_function	protein heterodimerization activity
D	0005737	cellular_component	cytoplasm
D	0005783	cellular_component	endoplasmic reticulum
D	0005829	cellular_component	cytosol
D	0006520	biological_process	amino acid metabolic process
D	0008615	biological_process	pyridoxine biosynthetic process
D	0009507	cellular_component	chloroplast
D	0016829	molecular_function	lyase activity
D	0016843	molecular_function	amine-lyase activity
D	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
D	0042819	biological_process	vitamin B6 biosynthetic process
D	0042823	biological_process	pyridoxal phosphate biosynthetic process
D	0046982	molecular_function	protein heterodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue KPR A 401

Chain	Residue
A	ASP41
A	GLY170
A	ALA229
A	GLY230
A	GLY231
A	PHE250
A	GLY252
A	SER253
A	HOH504
A	HOH509
A	HOH544
A	PRO66
A	LYS98
A	ASP119
A	SER121
A	VAL123
A	ARG164
A	GLU168
A	ALA169

---

site_id	AC2
Number of Residues	6
Details	binding site for residue PO4 A 402

Chain	Residue
A	HIS132
A	GLU151
A	ARG154
A	ARG155
A	HOH587
D	LYS204

---

site_id	AC3
Number of Residues	7
Details	binding site for residue PO4 B 402

Chain	Residue
B	HIS132
B	GLU151
B	ARG154
B	ARG155
B	HOH589
C	LYS204
C	HOH582

---

site_id	AC4
Number of Residues	7
Details	binding site for residue PO4 C 402

Chain	Residue
B	LYS204
C	HIS132
C	GLU151
C	ARG154
C	ARG155
C	HOH508
C	HOH588

---

site_id	AC5
Number of Residues	5
Details	binding site for residue PO4 D 402

Chain	Residue
A	LYS204
D	HIS132
D	GLU151
D	ARG154
D	ARG155

---

site_id	AC6
Number of Residues	26
Details	binding site for Di-peptide KPR B 401 and LYS B 98

Chain	Residue
B	ASP41
B	ALA61
B	LEU62
B	PRO66
B	MET78
B	ALA97
B	ALA99
B	LEU110
B	ASP119
B	SER121
B	VAL123
B	LEU124
B	ARG164
B	GLU168
B	ALA169
B	GLY170
B	ALA229
B	GLY230
B	GLY231
B	PHE250
B	GLY252
B	SER253
B	HOH511
B	HOH521
B	HOH524
B	HOH532

---

site_id	AC7
Number of Residues	27
Details	binding site for Di-peptide KPR C 401 and LYS C 98

Chain	Residue
C	ASP41
C	MET60
C	ALA61
C	LEU62
C	PRO66
C	MET78
C	ALA97
C	ALA99
C	ASP119
C	SER121
C	VAL123
C	LEU124
C	ARG164
C	GLU168
C	ALA169
C	GLY170
C	ALA229
C	GLY230
C	GLY231
C	PHE250
C	VAL251
C	GLY252
C	SER253
C	HOH510
C	HOH515
C	HOH530
C	HOH550

---

site_id	AC8
Number of Residues	26
Details	binding site for Di-peptide KPR D 401 and LYS D 98

Chain	Residue
D	ALA61
D	LEU62
D	PRO66
D	ALA97
D	ALA99
D	LEU110
D	ASP119
D	SER121
D	VAL123
D	LEU124
D	ARG164
D	GLU168
D	ALA169
D	GLY170
D	ALA229
D	GLY230
D	GLY231
D	PHE250
D	GLY252
D	SER253
D	HOH511
D	HOH515
D	HOH521
D	HOH559
D	ASP41
D	MET60

---

Functional Information from PROSITE/UniProt

site_id	PS01235
Number of Residues	19
Details	PDXS_SNZ_1 PdxS/SNZ family signature. LPVVQFAAGGVATPADAAL

Chain	Residue	Details
A	LEU222-LEU240

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Schiff-base intermediate with D-ribose 5-phosphate","evidences":[{"source":"UniProtKB","id":"O59080","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O59080","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q03148","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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