Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3GFB

L-Threonine Dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006566	biological_process	L-threonine metabolic process
A	0006567	biological_process	L-threonine catabolic process
A	0008270	molecular_function	zinc ion binding
A	0008743	molecular_function	L-threonine 3-dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016597	molecular_function	amino acid binding
A	0019518	biological_process	obsolete L-threonine catabolic process to glycine
A	0046872	molecular_function	metal ion binding
A	0051289	biological_process	protein homotetramerization
A	0070403	molecular_function	NAD+ binding
B	0005737	cellular_component	cytoplasm
B	0006566	biological_process	L-threonine metabolic process
B	0006567	biological_process	L-threonine catabolic process
B	0008270	molecular_function	zinc ion binding
B	0008743	molecular_function	L-threonine 3-dehydrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016597	molecular_function	amino acid binding
B	0019518	biological_process	obsolete L-threonine catabolic process to glycine
B	0046872	molecular_function	metal ion binding
B	0051289	biological_process	protein homotetramerization
B	0070403	molecular_function	NAD+ binding
C	0005737	cellular_component	cytoplasm
C	0006566	biological_process	L-threonine metabolic process
C	0006567	biological_process	L-threonine catabolic process
C	0008270	molecular_function	zinc ion binding
C	0008743	molecular_function	L-threonine 3-dehydrogenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016597	molecular_function	amino acid binding
C	0019518	biological_process	obsolete L-threonine catabolic process to glycine
C	0046872	molecular_function	metal ion binding
C	0051289	biological_process	protein homotetramerization
C	0070403	molecular_function	NAD+ binding
D	0005737	cellular_component	cytoplasm
D	0006566	biological_process	L-threonine metabolic process
D	0006567	biological_process	L-threonine catabolic process
D	0008270	molecular_function	zinc ion binding
D	0008743	molecular_function	L-threonine 3-dehydrogenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016597	molecular_function	amino acid binding
D	0019518	biological_process	obsolete L-threonine catabolic process to glycine
D	0046872	molecular_function	metal ion binding
D	0051289	biological_process	protein homotetramerization
D	0070403	molecular_function	NAD+ binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD A 500

Chain	Residue
A	GLY175
A	SER244
A	ALA246
A	ALA249
A	LEU266
A	GLY267
A	LEU268
A	ILE291
A	THR292
A	HOH404
A	HOH421
A	GLY177
A	HOH422
A	HOH425
A	HOH449
A	HOH562
B	ILE282
A	PRO178
A	LEU179
A	SER198
A	GLU199
A	PRO200
A	ARG204
A	PHE243

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD B 501

Chain	Residue
A	ILE282
B	GLY177
B	PRO178
B	LEU179
B	SER198
B	GLU199
B	PRO200
B	ARG204
B	PRO219
B	PHE243
B	SER244
B	ALA246
B	LEU266
B	LEU268
B	ILE291
B	THR292
B	HOH412
B	HOH414
B	HOH441
B	HOH446
B	HOH447

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 351

Chain	Residue
B	LEU162
B	GLY164
B	PRO165
C	PRO165

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 352

Chain	Residue
B	TYR147
B	GLY310
B	LEU312

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 353

Chain	Residue
B	ASP223
B	VAL225
B	GLN252
B	LYS255
B	HOH527

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 354

Chain	Residue
B	PRO247
B	GLU251
B	ARG271
B	VAL273
B	THR274

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 355

Chain	Residue
B	ARG271
B	GLU272
C	PRO270
C	ARG271

site_id	AC8
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD C 502

Chain	Residue
C	GLY175
C	GLY177
C	PRO178
C	LEU179
C	GLY180
C	SER198
C	GLU199
C	PRO200
C	ARG204
C	PHE243
C	SER244
C	ALA246
C	ALA249
C	LEU266
C	GLY267
C	LEU268
C	ILE291
C	THR292
C	HOH411
C	HOH451
C	HOH453
C	HOH455
C	HOH456
C	HOH457
C	HOH615
D	ILE282

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 351

Chain	Residue
C	PRO78
C	GLY79
C	GLU81

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 352

Chain	Residue
C	VAL257
C	MET229
C	GLY234
C	ALA235
C	LYS255

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 353

Chain	Residue
C	VAL158
C	ASP159
C	LEU162
C	GLU298
C	THR299
C	THR302

site_id	BC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD D 503

Chain	Residue
C	ILE282
D	GLY175
D	GLY177
D	PRO178
D	LEU179
D	GLY180
D	SER198
D	GLU199
D	PRO200
D	ARG204
D	PRO219
D	PHE243
D	SER244
D	ALA246
D	LEU266
D	GLY267
D	LEU268
D	ILE291
D	THR292
D	HOH360
D	HOH361
D	HOH374
D	HOH419
D	HOH443
D	HOH444
D	HOH633
D	HOH634

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 351

Chain	Residue
A	ARG271
A	GLU272
D	ARG271
D	HOH610

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 352

Chain	Residue
A	PRO270
A	ARG271
D	ARG271
D	GLU272

Functional Information from PROSITE/UniProt

site_id	PS00059
Number of Residues	15
Details	ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEvAGEvvevGpgV

Chain	Residue	Details
A	GLY66-VAL80

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"HAMAP-Rule","id":"MF_00627","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00627","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19616102","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19616102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3GFB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom","evidences":[{"source":"HAMAP-Rule","id":"MF_00627","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	THR44
A	GLY43

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

Chain	Residue	Details
B	THR44
B	GLY43

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

Chain	Residue	Details
C	THR44
C	GLY43

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

Chain	Residue	Details
D	THR44
D	GLY43

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

Chain	Residue	Details
A	THR44
A	HIS47

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

Chain	Residue	Details
B	THR44
B	HIS47

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1teh

Chain	Residue	Details
C	THR44
C	HIS47

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1teh

Chain	Residue	Details
D	THR44
D	HIS47

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