Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1EBU

HOMOSERINE DEHYDROGENASE COMPLEX WITH NAD ANALOGUE AND L-HOMOSERINE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004412	molecular_function	homoserine dehydrogenase activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0006520	biological_process	amino acid metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0009067	biological_process	aspartate family amino acid biosynthetic process
A	0009086	biological_process	methionine biosynthetic process
A	0009088	biological_process	threonine biosynthetic process
A	0009090	biological_process	homoserine biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0050661	molecular_function	NADP binding
A	0070403	molecular_function	NAD+ binding
B	0004412	molecular_function	homoserine dehydrogenase activity
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0006520	biological_process	amino acid metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0009067	biological_process	aspartate family amino acid biosynthetic process
B	0009086	biological_process	methionine biosynthetic process
B	0009088	biological_process	threonine biosynthetic process
B	0009090	biological_process	homoserine biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0050661	molecular_function	NADP binding
B	0070403	molecular_function	NAD+ binding
C	0004412	molecular_function	homoserine dehydrogenase activity
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0006520	biological_process	amino acid metabolic process
C	0008652	biological_process	amino acid biosynthetic process
C	0009067	biological_process	aspartate family amino acid biosynthetic process
C	0009086	biological_process	methionine biosynthetic process
C	0009088	biological_process	threonine biosynthetic process
C	0009090	biological_process	homoserine biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0050661	molecular_function	NADP binding
C	0070403	molecular_function	NAD+ binding
D	0004412	molecular_function	homoserine dehydrogenase activity
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0006520	biological_process	amino acid metabolic process
D	0008652	biological_process	amino acid biosynthetic process
D	0009067	biological_process	aspartate family amino acid biosynthetic process
D	0009086	biological_process	methionine biosynthetic process
D	0009088	biological_process	threonine biosynthetic process
D	0009090	biological_process	homoserine biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0050661	molecular_function	NADP binding
D	0070403	molecular_function	NAD+ binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 901

Chain	Residue
A	GLU143
A	GLY147
A	ALA148
A	LEU150

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA B 902

Chain	Residue
B	GLU143
B	VAL146
B	ALA148
B	LEU150

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA C 903

Chain	Residue
C	VAL146
C	GLY147
C	ALA148
C	GLY149
C	LEU150
C	GLU143

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA D 904

Chain	Residue
D	GLU143
D	VAL146
D	ALA148
D	LEU150

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NDA D 1300

Chain	Residue
D	GLY12
D	ALA13
D	GLY14
D	VAL15
D	VAL16
D	GLY17
D	GLU40
D	ALA41
D	ASN92
D	THR93
D	SER94
D	PRO115
D	LYS117
D	GLY338
D	ALA339
D	GLY340
D	THR344
D	HSE1301

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HSE D 1301

Chain	Residue
D	GLU208
D	ASP219
D	NDA1300

Functional Information from PROSITE/UniProt

site_id	PS01042
Number of Residues	23
Details	HOMOSER_DHGENASE Homoserine dehydrogenase signature. AkklGYTep.DPrdDLnGlDvarK

Chain	Residue	Details
A	ALA201-LYS223

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PIRSR","id":"PIRSR036497-1","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10700284","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EBU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O58802","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10700284","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EBF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10700284","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14583265","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q7G","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"F9VNG5","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10700284","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EBU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ebf

Chain	Residue	Details
A	LYS223
A	ASP219

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ebf

Chain	Residue	Details
B	LYS223
B	ASP219

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ebf

Chain	Residue	Details
C	LYS223
C	ASP219

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

Chain	Residue	Details
D	LYS223
D	ASP219

site_id	MCSA1
Number of Residues	2
Details	M-CSA 521

Chain	Residue	Details
A	ASP219	electrostatic stabiliser
A	LYS223	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	2
Details	M-CSA 521

Chain	Residue	Details
B	ASP219	electrostatic stabiliser
B	LYS223	proton shuttle (general acid/base)

site_id	MCSA3
Number of Residues	2
Details	M-CSA 521

Chain	Residue	Details
C	ASP219	electrostatic stabiliser
C	LYS223	proton shuttle (general acid/base)

site_id	MCSA4
Number of Residues	2
Details	M-CSA 521

Chain	Residue	Details
D	ASP219	electrostatic stabiliser
D	LYS223	proton shuttle (general acid/base)

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