Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2C2B

Crystallographic structure of Arabidopsis thaliana Threonine synthase complexed with pyridoxal phosphate and S-adenosylmethionine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004795	molecular_function	threonine synthase activity
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0006520	biological_process	amino acid metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0009088	biological_process	threonine biosynthetic process
A	0009507	cellular_component	chloroplast
A	0009570	cellular_component	chloroplast stroma
A	0010073	biological_process	meristem maintenance
A	0016829	molecular_function	lyase activity
A	0019344	biological_process	cysteine biosynthetic process
A	0030170	molecular_function	pyridoxal phosphate binding
B	0003824	molecular_function	catalytic activity
B	0004795	molecular_function	threonine synthase activity
B	0005737	cellular_component	cytoplasm
B	0005886	cellular_component	plasma membrane
B	0006520	biological_process	amino acid metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0009088	biological_process	threonine biosynthetic process
B	0009507	cellular_component	chloroplast
B	0009570	cellular_component	chloroplast stroma
B	0010073	biological_process	meristem maintenance
B	0016829	molecular_function	lyase activity
B	0019344	biological_process	cysteine biosynthetic process
B	0030170	molecular_function	pyridoxal phosphate binding
C	0003824	molecular_function	catalytic activity
C	0004795	molecular_function	threonine synthase activity
C	0005737	cellular_component	cytoplasm
C	0005886	cellular_component	plasma membrane
C	0006520	biological_process	amino acid metabolic process
C	0008652	biological_process	amino acid biosynthetic process
C	0009088	biological_process	threonine biosynthetic process
C	0009507	cellular_component	chloroplast
C	0009570	cellular_component	chloroplast stroma
C	0010073	biological_process	meristem maintenance
C	0016829	molecular_function	lyase activity
C	0019344	biological_process	cysteine biosynthetic process
C	0030170	molecular_function	pyridoxal phosphate binding
D	0003824	molecular_function	catalytic activity
D	0004795	molecular_function	threonine synthase activity
D	0005737	cellular_component	cytoplasm
D	0005886	cellular_component	plasma membrane
D	0006520	biological_process	amino acid metabolic process
D	0008652	biological_process	amino acid biosynthetic process
D	0009088	biological_process	threonine biosynthetic process
D	0009507	cellular_component	chloroplast
D	0009570	cellular_component	chloroplast stroma
D	0010073	biological_process	meristem maintenance
D	0016829	molecular_function	lyase activity
D	0019344	biological_process	cysteine biosynthetic process
D	0030170	molecular_function	pyridoxal phosphate binding
E	0003824	molecular_function	catalytic activity
E	0004795	molecular_function	threonine synthase activity
E	0005737	cellular_component	cytoplasm
E	0005886	cellular_component	plasma membrane
E	0006520	biological_process	amino acid metabolic process
E	0008652	biological_process	amino acid biosynthetic process
E	0009088	biological_process	threonine biosynthetic process
E	0009507	cellular_component	chloroplast
E	0009570	cellular_component	chloroplast stroma
E	0010073	biological_process	meristem maintenance
E	0016829	molecular_function	lyase activity
E	0019344	biological_process	cysteine biosynthetic process
E	0030170	molecular_function	pyridoxal phosphate binding
F	0003824	molecular_function	catalytic activity
F	0004795	molecular_function	threonine synthase activity
F	0005737	cellular_component	cytoplasm
F	0005886	cellular_component	plasma membrane
F	0006520	biological_process	amino acid metabolic process
F	0008652	biological_process	amino acid biosynthetic process
F	0009088	biological_process	threonine biosynthetic process
F	0009507	cellular_component	chloroplast
F	0009570	cellular_component	chloroplast stroma
F	0010073	biological_process	meristem maintenance
F	0016829	molecular_function	lyase activity
F	0019344	biological_process	cysteine biosynthetic process
F	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP A 1163

Chain	Residue
A	PHE162
A	ALA356
A	HIS404
A	THR432
A	ALA433
A	HOH2025
A	LYS163
A	ASP194
A	GLY294
A	GLY295
A	ASN296
A	LEU297
A	GLY298
A	ASN299

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PLP B 1163

Chain	Residue
B	LYS163
B	SER191
B	THR195
B	SER262
B	ARG267
B	GLN271
B	ASN296
B	ASN299

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP C 1163

Chain	Residue
C	PHE162
C	LYS163
C	ASP194
C	GLY294
C	GLY295
C	ASN296
C	LEU297
C	GLY298
C	ASN299
C	ALA356
C	HIS404
C	THR432
C	ALA433
C	HOH2038

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PLP D 1163

Chain	Residue
D	PHE162
D	LYS163
D	SER191
D	ASP194
D	THR195
D	SER262
D	ARG267
D	GLN271
D	ASN296
D	ASN299

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PLP E 1163

Chain	Residue
E	PHE162
E	LYS163
E	SER191
E	ASP194
E	THR195
E	SER262
E	ARG267
E	GLN271
E	ASN296
E	ASN299

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP F 1163

Chain	Residue
F	PHE162
F	LYS163
F	ASP194
F	GLY294
F	GLY295
F	ASN296
F	LEU297
F	GLY298
F	ASN299
F	ALA356
F	HIS404
F	THR432
F	ALA433
F	HOH2046

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE SAM A 500

Chain	Residue
A	SER99
A	THR100
A	TRP101
A	PRO102
A	GLY104
A	SER105
A	SER125
A	PHE127
A	SAM501
B	ASN132
B	LEU133
B	TRP150
B	GLN281
B	PHE282

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SAM A 501

Chain	Residue
A	TRP101
A	SAM500
A	HOH2051
B	TRP135
B	LYS141
B	ASN147
B	TRP150

site_id	AC9
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SAM B 500

Chain	Residue
B	GLY104
B	SER105
B	SER125
B	PHE127
B	SAM501
A	ASN132
A	LEU133
A	TRP150
A	GLN281
B	SER99
B	THR100
B	TRP101
B	PRO102

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SAM B 501

Chain	Residue
A	TRP135
A	LYS141
A	ASN147
A	TRP150
B	TRP101
B	SAM500
B	HOH2055
E	ASP343

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE SAM C 500

Chain	Residue
C	SER99
C	THR100
C	TRP101
C	PRO102
C	GLY104
C	SER105
C	SER125
C	PHE127
C	SAM501
D	ASN132
D	LEU133
D	TRP150
D	GLN281
D	PHE282

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SAM C 501

Chain	Residue
C	TRP101
C	SAM500
C	HOH2051
C	HOH2052
D	TRP135
D	LYS141
D	ASN147
D	TRP150

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE SAM D 500

Chain	Residue
C	ASN132
C	LEU133
C	TRP150
C	GLN281
C	PHE282
D	SER99
D	THR100
D	TRP101
D	PRO102
D	GLY104
D	SER105
D	SER125
D	PHE127
D	SAM501

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SAM D 501

Chain	Residue
C	TRP135
C	LYS141
C	TRP150
D	TRP101
D	ASP343
D	SAM500
D	HOH2054

site_id	BC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SAM E 500

Chain	Residue
E	SER99
E	THR100
E	TRP101
E	PRO102
E	GLY104
E	SER125
E	PHE127
E	SAM501
F	ASN132
F	LEU133
F	TRP150
F	GLN281
F	ASP283

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SAM E 501

Chain	Residue
B	ASP343
E	TRP101
E	SAM500
E	HOH2044
F	TRP135
F	LYS141
F	ASN147

site_id	BC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE SAM F 500

Chain	Residue
E	ASN132
E	LEU133
E	TRP150
E	GLN281
E	PHE282
F	SER99
F	THR100
F	TRP101
F	PRO102
F	TYR103
F	GLY104
F	SER105
F	SER125
F	PHE127
F	SAM501

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SAM F 501

Chain	Residue
E	TRP135
E	LYS141
E	ASN147
E	TRP150
F	TRP101
F	SAM500
F	HOH2056

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE TRS A 800

Chain	Residue
A	ASP122

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRS C 800

Chain	Residue
C	ASP119
C	ASP122

site_id	CC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRS F 800

Chain	Residue
F	ASP119
F	ASP122

Functional Information from PROSITE/UniProt

site_id	PS00165
Number of Residues	15
Details	DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. HcgishTGSFKDLGM

Chain	Residue	Details
A	HIS153-MET167

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16319072","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"description":"in monomer A","evidences":[{"source":"PubMed","id":"16319072","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"description":"in monomer B","evidences":[{"source":"PubMed","id":"16319072","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	30
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	SER431

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

Chain	Residue	Details
B	SER431

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

Chain	Residue	Details
C	SER431

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

Chain	Residue	Details
D	SER431

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

Chain	Residue	Details
E	SER431

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

Chain	Residue	Details
F	SER431

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