Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ADS

Crystal structure of plasmodial PLP synthase complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0042819	biological_process	vitamin B6 biosynthetic process
A	0042823	biological_process	pyridoxal phosphate biosynthetic process
B	0042819	biological_process	vitamin B6 biosynthetic process
B	0042823	biological_process	pyridoxal phosphate biosynthetic process
C	0042819	biological_process	vitamin B6 biosynthetic process
C	0042823	biological_process	pyridoxal phosphate biosynthetic process
D	0042819	biological_process	vitamin B6 biosynthetic process
D	0042823	biological_process	pyridoxal phosphate biosynthetic process
E	0042819	biological_process	vitamin B6 biosynthetic process
E	0042823	biological_process	pyridoxal phosphate biosynthetic process
F	0042819	biological_process	vitamin B6 biosynthetic process
F	0042823	biological_process	pyridoxal phosphate biosynthetic process
G	0000304	biological_process	response to singlet oxygen
G	0004359	molecular_function	glutaminase activity
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0008614	biological_process	pyridoxine metabolic process
G	0016787	molecular_function	hydrolase activity
G	0016829	molecular_function	lyase activity
G	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
G	0042819	biological_process	vitamin B6 biosynthetic process
G	0042823	biological_process	pyridoxal phosphate biosynthetic process
G	1903600	cellular_component	glutaminase complex
H	0000304	biological_process	response to singlet oxygen
H	0004359	molecular_function	glutaminase activity
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0008614	biological_process	pyridoxine metabolic process
H	0016787	molecular_function	hydrolase activity
H	0016829	molecular_function	lyase activity
H	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
H	0042819	biological_process	vitamin B6 biosynthetic process
H	0042823	biological_process	pyridoxal phosphate biosynthetic process
H	1903600	cellular_component	glutaminase complex
I	0000304	biological_process	response to singlet oxygen
I	0004359	molecular_function	glutaminase activity
I	0005737	cellular_component	cytoplasm
I	0005829	cellular_component	cytosol
I	0008614	biological_process	pyridoxine metabolic process
I	0016787	molecular_function	hydrolase activity
I	0016829	molecular_function	lyase activity
I	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
I	0042819	biological_process	vitamin B6 biosynthetic process
I	0042823	biological_process	pyridoxal phosphate biosynthetic process
I	1903600	cellular_component	glutaminase complex
J	0000304	biological_process	response to singlet oxygen
J	0004359	molecular_function	glutaminase activity
J	0005737	cellular_component	cytoplasm
J	0005829	cellular_component	cytosol
J	0008614	biological_process	pyridoxine metabolic process
J	0016787	molecular_function	hydrolase activity
J	0016829	molecular_function	lyase activity
J	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
J	0042819	biological_process	vitamin B6 biosynthetic process
J	0042823	biological_process	pyridoxal phosphate biosynthetic process
J	1903600	cellular_component	glutaminase complex
K	0000304	biological_process	response to singlet oxygen
K	0004359	molecular_function	glutaminase activity
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0008614	biological_process	pyridoxine metabolic process
K	0016787	molecular_function	hydrolase activity
K	0016829	molecular_function	lyase activity
K	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
K	0042819	biological_process	vitamin B6 biosynthetic process
K	0042823	biological_process	pyridoxal phosphate biosynthetic process
K	1903600	cellular_component	glutaminase complex
L	0000304	biological_process	response to singlet oxygen
L	0004359	molecular_function	glutaminase activity
L	0005737	cellular_component	cytoplasm
L	0005829	cellular_component	cytosol
L	0008614	biological_process	pyridoxine metabolic process
L	0016787	molecular_function	hydrolase activity
L	0016829	molecular_function	lyase activity
L	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
L	0042819	biological_process	vitamin B6 biosynthetic process
L	0042823	biological_process	pyridoxal phosphate biosynthetic process
L	1903600	cellular_component	glutaminase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 301

Chain	Residue
A	HIS118
A	ARG140
A	ARG141
E	LYS190

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 302

Chain	Residue
A	GLY156
A	GLY216
A	GLY217
A	GLY238
A	SER239

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 301

Chain	Residue
B	HIS118
B	ARG140
B	ARG141
D	LYS190

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 302

Chain	Residue
B	GLY156
B	GLY217
B	VAL237
B	GLY238
B	SER239

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 301

Chain	Residue
C	HIS118
C	ARG140
C	ARG141
C	LYS190

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 302

Chain	Residue
C	GLY156
C	GLY216
C	GLY217
C	GLY238
C	SER239

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 301

Chain	Residue
B	LYS190
D	HIS118
D	ARG140
D	ARG141

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 D 302

Chain	Residue
D	GLY156
D	GLY216
D	GLY217
D	GLY238
D	SER239

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 E 301

Chain	Residue
A	LYS190
E	HIS118
E	ARG140
E	ARG141

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 E 302

Chain	Residue
E	GLY156
E	GLY216
E	GLY217
E	GLY238
E	SER239

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 F 301

Chain	Residue
F	HIS118
F	ARG140
F	ARG141
F	LYS190

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 F 302

Chain	Residue
F	GLY156
F	GLY217
F	VAL237
F	GLY238
F	SER239

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU208-MET226

site_id	PS01236
Number of Residues	11
Details	PDXT_SNO_1 PdxT/SNO family family signature. GLVIPGGESTT

Chain	Residue	Details
G	GLY46-THR56

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P37528","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"P37528","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P37528","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)