Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2ISS

Structure of the PLP synthase Holoenzyme from Thermotoga maritima

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006520	biological_process	amino acid metabolic process
A	0008615	biological_process	pyridoxine biosynthetic process
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
B	0006520	biological_process	amino acid metabolic process
B	0008615	biological_process	pyridoxine biosynthetic process
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
C	0006520	biological_process	amino acid metabolic process
C	0008615	biological_process	pyridoxine biosynthetic process
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
D	0004359	molecular_function	glutaminase activity
D	0005829	cellular_component	cytosol
D	0006543	biological_process	L-glutamine catabolic process
D	0008614	biological_process	pyridoxine metabolic process
D	0016787	molecular_function	hydrolase activity
D	0016829	molecular_function	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	1903600	cellular_component	glutaminase complex
E	0004359	molecular_function	glutaminase activity
E	0005829	cellular_component	cytosol
E	0006543	biological_process	L-glutamine catabolic process
E	0008614	biological_process	pyridoxine metabolic process
E	0016787	molecular_function	hydrolase activity
E	0016829	molecular_function	lyase activity
E	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
E	0042819	biological_process	vitamin B6 biosynthetic process
E	0042823	biological_process	pyridoxal phosphate biosynthetic process
E	1903600	cellular_component	glutaminase complex
F	0004359	molecular_function	glutaminase activity
F	0005829	cellular_component	cytosol
F	0006543	biological_process	L-glutamine catabolic process
F	0008614	biological_process	pyridoxine metabolic process
F	0016787	molecular_function	hydrolase activity
F	0016829	molecular_function	lyase activity
F	0036381	molecular_function	pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
F	0042819	biological_process	vitamin B6 biosynthetic process
F	0042823	biological_process	pyridoxal phosphate biosynthetic process
F	1903600	cellular_component	glutaminase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 5RP A 294

Chain	Residue
A	ASP25
A	GLY154
A	GLY214
A	GLY215
A	GLY236
A	SER237
A	MET44
A	PRO50
A	LYS82
A	ASP103
A	VAL107
A	ARG148
A	GLU152
A	ALA153

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 5RP B 294

Chain	Residue
B	ASP25
B	MET44
B	PRO50
B	LYS82
B	ASP103
B	VAL107
B	ARG148
B	GLU152
B	ALA153
B	GLY154
B	GLY214
B	GLY215
B	GLY236
B	SER237

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 5RP C 294

Chain	Residue
C	ASP25
C	MET44
C	PRO50
C	LYS82
C	ASP103
C	VAL107
C	ARG148
C	GLU152
C	ALA153
C	GLY154
C	GLY214
C	GLY215
C	GLY236
C	SER237

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 300

Chain	Residue
A	HIS116
A	ARG138
A	ARG139
A	LYS188

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

Chain	Residue
B	HIS116
B	ARG138
B	ARG139
C	LYS188

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 302

Chain	Residue
B	LYS188
C	HIS116
C	ARG138
C	ARG139

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU206-LEU224

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

Chain	Residue	Details
D	GLY40-THR50

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Nucleophile => ECO:0000255\|HAMAP-Rule:MF_01615

Chain	Residue	Details
D	CYS78
E	CYS78
F	CYS78

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: Charge relay system => ECO:0000255\|HAMAP-Rule:MF_01615

Chain	Residue	Details
D	HIS170
C	GLY154
C	GLY215
C	GLY236
D	GLU172
E	HIS170
E	GLU172
F	HIS170
F	GLU172
B	GLY215
B	GLY236
C	ASP25

site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01615

Chain	Residue	Details
D	GLY46
D	ARG105
D	ILE134
E	GLY46
E	ARG105
E	ILE134
F	GLY46
F	ARG105
F	ILE134

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01824

Chain	Residue	Details
A	ARG166
B	ARG166
C	ARG166

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
F	GLU172
F	HIS170
F	CYS78

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
D	GLU172
D	HIS170
D	CYS78

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
E	GLU172
E	HIS170
E	CYS78

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
D	HIS170
D	CYS78

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
E	HIS170
E	CYS78

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
F	HIS170
F	CYS78

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