Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1ZNN

Structure of the synthase subunit of PLP synthase

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	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	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	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	0006520	biological_process	amino acid metabolic process
D	0008615	biological_process	pyridoxine biosynthetic process
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
E	0006520	biological_process	amino acid metabolic process
E	0008615	biological_process	pyridoxine biosynthetic process
E	0016843	molecular_function	amine-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
F	0006520	biological_process	amino acid metabolic process
F	0008615	biological_process	pyridoxine biosynthetic process
F	0016843	molecular_function	amine-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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 2401

Chain	Residue
A	HIS115
A	ARG137
A	ARG138
A	HOH3097
C	LYS187

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 A 2402

Chain	Residue
A	GLY214
A	MRD2888
A	HOH2934
A	HOH2940
A	HOH2950
A	HOH2968
A	HOH3213
A	PRO152
A	GLY153
A	THR154
A	GLY155

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 2403

Chain	Residue
B	GLU134
B	ARG137
B	ARG138
B	LYS187
B	HOH2993
B	HOH3002
B	HOH3149
B	HOH3186

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 B 2404

Chain	Residue
B	PRO152
B	GLY153
B	THR154
B	GLY155
B	GLY214
B	HOH2933
B	HOH2966
B	HOH2974
B	HOH2980
B	HOH3219
B	HOH3235

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 2405

Chain	Residue
A	LYS187
C	HIS115
C	GLU134
C	ARG137
C	ARG138
C	HOH2933

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 C 2406

Chain	Residue
C	PRO152
C	GLY153
C	THR154
C	GLY155
C	GLY213
C	GLY214
C	MRD2890
C	HOH2939
C	HOH3005
C	HOH3078
C	HOH3133

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 2407

Chain	Residue
D	HIS115
D	GLU134
D	ARG137
D	ARG138
D	HOH3012
D	HOH3020
F	LYS187

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 D 2408

Chain	Residue
D	PRO152
D	GLY153
D	THR154
D	GLY155
D	GLY213
D	GLY214
D	HOH2951
D	HOH2957
D	HOH3021
D	HOH3031

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 2409

Chain	Residue
E	HIS115
E	ARG137
E	ARG138
E	LYS187
E	HOH2995
E	HOH3025

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 E 2410

Chain	Residue
E	GLY153
E	THR154
E	GLY155
E	GLY213
E	GLY214
E	HOH2913
E	HOH2924
E	HOH2970
E	HOH3000

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 2411

Chain	Residue
D	LYS187
F	GLU134
F	ARG137
F	ARG138
F	HOH3016
F	HOH3044

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 F 2412

Chain	Residue
F	HOH3036
F	PRO152
F	GLY153
F	THR154
F	GLY155
F	GLY213
F	GLY214
F	MRD2893
F	HOH2966
F	HOH2975

site_id	BC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MRD A 2888

Chain	Residue
A	ASP24
A	LYS81
A	ASP102
A	GLY213
A	PHE233
A	VAL234
A	GLY235
A	SO42402
A	HOH2934
A	HOH2963

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MRD B 2889

Chain	Residue
B	ASP24
B	LYS81
B	ASP102
B	GLY213
B	PHE233
B	VAL234
B	GLY235
B	HOH2952
B	HOH2974

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MRD C 2890

Chain	Residue
C	ASP24
C	LYS81
C	ASP102
C	GLY213
C	PHE233
C	VAL234
C	SO42406
C	HOH3005
C	HOH3009
C	HOH3133

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MRD D 2891

Chain	Residue
D	ASP24
D	LYS81
D	ASP102
D	GLY213
D	PHE233
D	VAL234
D	GLY235
D	HOH2951

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MRD E 2892

Chain	Residue
E	ASP24
E	LYS81
E	ASP102
E	GLY213
E	PHE233
E	VAL234
E	GLY235
E	HOH2932

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MRD F 2893

Chain	Residue
F	ASP24
F	LYS81
F	ASP102
F	GLY213
F	PHE233
F	VAL234
F	GLY235
F	SO42412
F	HOH2962

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU205-LEU223

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Schiff-base intermediate with D-ribose 5-phosphate","evidences":[{"source":"HAMAP-Rule","id":"MF_01824","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15911615","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01824","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15911615","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01824","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1g4p

Chain	Residue	Details
A	GLY128

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1g4p

Chain	Residue	Details
B	GLY128

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1g4p

Chain	Residue	Details
C	GLY128

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1g4p

Chain	Residue	Details
D	GLY128

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1g4p

Chain	Residue	Details
E	GLY128

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1g4p

Chain	Residue	Details
F	GLY128

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