Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CJ0

CRYSTAL STRUCTURE OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE AT 2.8 ANGSTROM RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000900	molecular_function	mRNA regulatory element binding translation repressor activity
A	0004372	molecular_function	glycine hydroxymethyltransferase activity
A	0004793	molecular_function	threonine aldolase activity
A	0005521	molecular_function	lamin binding
A	0005634	cellular_component	nucleus
A	0005657	cellular_component	replication fork
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
A	0006231	biological_process	dTMP biosynthetic process
A	0006260	biological_process	DNA replication
A	0006544	biological_process	glycine metabolic process
A	0006563	biological_process	L-serine metabolic process
A	0006565	biological_process	L-serine catabolic process
A	0006730	biological_process	one-carbon metabolic process
A	0008732	molecular_function	L-allo-threonine aldolase activity
A	0009113	biological_process	purine nucleobase biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016829	molecular_function	lyase activity
A	0017148	biological_process	negative regulation of translation
A	0019264	biological_process	glycine biosynthetic process from L-serine
A	0030170	molecular_function	pyridoxal phosphate binding
A	0035999	biological_process	tetrahydrofolate interconversion
A	0036094	molecular_function	small molecule binding
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0044281	biological_process	small molecule metabolic process
A	0046653	biological_process	tetrahydrofolate metabolic process
A	0046655	biological_process	folic acid metabolic process
A	0048027	molecular_function	mRNA 5'-UTR binding
A	0050179	molecular_function	phenylserine aldolase activity
A	0051289	biological_process	protein homotetramerization
A	0070905	molecular_function	serine binding
A	0120567	molecular_function	hydroxytrimethyllysine aldolase activity
A	1904482	biological_process	cellular response to tetrahydrofolate
B	0000900	molecular_function	mRNA regulatory element binding translation repressor activity
B	0004372	molecular_function	glycine hydroxymethyltransferase activity
B	0004793	molecular_function	threonine aldolase activity
B	0005521	molecular_function	lamin binding
B	0005634	cellular_component	nucleus
B	0005657	cellular_component	replication fork
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
B	0006231	biological_process	dTMP biosynthetic process
B	0006260	biological_process	DNA replication
B	0006544	biological_process	glycine metabolic process
B	0006563	biological_process	L-serine metabolic process
B	0006565	biological_process	L-serine catabolic process
B	0006730	biological_process	one-carbon metabolic process
B	0008732	molecular_function	L-allo-threonine aldolase activity
B	0009113	biological_process	purine nucleobase biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016829	molecular_function	lyase activity
B	0017148	biological_process	negative regulation of translation
B	0019264	biological_process	glycine biosynthetic process from L-serine
B	0030170	molecular_function	pyridoxal phosphate binding
B	0035999	biological_process	tetrahydrofolate interconversion
B	0036094	molecular_function	small molecule binding
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0044281	biological_process	small molecule metabolic process
B	0046653	biological_process	tetrahydrofolate metabolic process
B	0046655	biological_process	folic acid metabolic process
B	0048027	molecular_function	mRNA 5'-UTR binding
B	0050179	molecular_function	phenylserine aldolase activity
B	0051289	biological_process	protein homotetramerization
B	0070905	molecular_function	serine binding
B	0120567	molecular_function	hydroxytrimethyllysine aldolase activity
B	1904482	biological_process	cellular response to tetrahydrofolate

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP A 2291

Chain	Residue
A	SER97
A	GLY98
A	SER99
A	HIS126
A	SER175
A	ASP200
A	ALA202
A	HIS203
A	THR226
A	HIS228
A	LYS229
B	TYR55
B	GLY262
B	GLY263

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP B 2291

Chain	Residue
A	TYR55
A	GLY262
A	GLY263
B	SER97
B	GLY98
B	SER99
B	HIS126
B	THR174
B	SER175
B	ASP200
B	ALA202
B	HIS203
B	THR226
B	HIS228
B	LYS229

site_id	CTA
Number of Residues	6
Details	RESIDUES COMPRISING ACTIVE SITE FOR MOLECULE A

Chain	Residue
B	GLU57
B	TYR65
B	ARG363
A	HIS126
A	THR226
A	HIS228

site_id	CTB
Number of Residues	6
Details	RESIDUES COMPRISING ACTIVE SITE FOR MOLECULE B

Chain	Residue
B	HIS126
B	THR226
B	HIS228
A	GLU57
A	TYR65
A	ARG363

Functional Information from PROSITE/UniProt

site_id	PS00096
Number of Residues	17
Details	SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVvTTTTHKTLrGCRAG

Chain	Residue	Details
A	HIS221-GLY237

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15170323","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12438316","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15170323","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RV3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10387080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12438316","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15170323","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RV3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RV4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12438316","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LS3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12438316","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15170323","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RV3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RV4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12438316","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15170323","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RV3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RV4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P50431","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10387080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12438316","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15170323","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RV3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RV4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15170323","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RV4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10387080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12438316","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15170323","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10387080","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RV3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RV4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RVY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1; alternate)","evidences":[{"source":"UniProtKB","id":"P34896","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin; alternate)","evidences":[{"source":"UniProtKB","id":"P34896","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	ARG63

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

Chain	Residue	Details
B	ARG63

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

Chain	Residue	Details
A	THR226
A	LYS229
A	GLU57

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1dfo

Chain	Residue	Details
B	THR226
B	LYS229
B	GLU57

site_id	MCSA1
Number of Residues	6
Details	M-CSA 147

Chain	Residue	Details
A	TYR55	steric locator
A	GLU57	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASP200	electrostatic stabiliser
A	THR226	electrostatic stabiliser, hydrogen bond acceptor
A	LYS229	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	ARG235	electrostatic stabiliser

site_id	MCSA2
Number of Residues	6
Details	M-CSA 147

Chain	Residue	Details
B	TYR55	steric locator
B	GLU57	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASP200	electrostatic stabiliser
B	THR226	electrostatic stabiliser, hydrogen bond acceptor
B	LYS229	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
B	ARG235	electrostatic stabiliser

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