Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3FLK

Crystal Structure of Tartrate Dehydrogenase from Pseudomonas putida in complex with NADH, oxalate and metal ion

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005737	cellular_component	cytoplasm
A	0009027	molecular_function	tartrate dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0016829	molecular_function	lyase activity
A	0046553	molecular_function	D-malate dehydrogenase (decarboxylating) (NAD+) activity
A	0046872	molecular_function	metal ion binding
A	0050319	molecular_function	tartrate decarboxylase activity
A	0051287	molecular_function	NAD binding
B	0000287	molecular_function	magnesium ion binding
B	0005737	cellular_component	cytoplasm
B	0009027	molecular_function	tartrate dehydrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0016829	molecular_function	lyase activity
B	0046553	molecular_function	D-malate dehydrogenase (decarboxylating) (NAD+) activity
B	0046872	molecular_function	metal ion binding
B	0050319	molecular_function	tartrate decarboxylase activity
B	0051287	molecular_function	NAD binding
C	0000287	molecular_function	magnesium ion binding
C	0005737	cellular_component	cytoplasm
C	0009027	molecular_function	tartrate dehydrogenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0016829	molecular_function	lyase activity
C	0046553	molecular_function	D-malate dehydrogenase (decarboxylating) (NAD+) activity
C	0046872	molecular_function	metal ion binding
C	0050319	molecular_function	tartrate decarboxylase activity
C	0051287	molecular_function	NAD binding
D	0000287	molecular_function	magnesium ion binding
D	0005737	cellular_component	cytoplasm
D	0009027	molecular_function	tartrate dehydrogenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0016829	molecular_function	lyase activity
D	0046553	molecular_function	D-malate dehydrogenase (decarboxylating) (NAD+) activity
D	0046872	molecular_function	metal ion binding
D	0050319	molecular_function	tartrate decarboxylase activity
D	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	ASP250
A	OXL403
A	HOH665
A	HOH666
B	ASP225

site_id	AC2
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAI A 402

Chain	Residue
A	GLY79
A	PRO81
A	ASP86
A	LEU94
A	ILE263
A	GLU282
A	HIS285
A	GLY286
A	SER287
A	ALA288
A	ILE291
A	ASN298
A	OXL403
A	NH4404
A	HOH505
A	HOH517
A	HOH520
A	HOH531
A	HOH548
A	HOH619
A	HOH631
A	HOH667
A	HOH668
A	HOH669
A	HOH671
B	ASN194
B	HIS223
B	ILE226
B	ARG230
A	ILE16
A	PHE75
A	ALA77
A	VAL78

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OXL A 403

Chain	Residue
A	ARG98
A	ARG108
A	ARG134
A	ASP250
A	MG401
A	NAI402
A	HOH600
B	LYS192
B	ASP225

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NH4 A 404

Chain	Residue
A	GLY76
A	GLU282
A	PRO283
A	HIS285
A	NAI402

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 405

Chain	Residue
A	ASP225
B	ASP250
B	OXL402
B	HOH659
B	HOH660

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 406

Chain	Residue
A	ARG111
A	TRP304
A	LEU308
A	HIS324
A	LEU328
A	HOH721

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 407

Chain	Residue
A	GLN234
A	ARG237
C	ARG7

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 408

Chain	Residue
A	LYS57
A	PRO60
A	ASP61
A	ASP62
A	HOH693

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 409

Chain	Residue
A	ARG182
A	GLU183
A	HOH547

site_id	BC1
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAI B 401

Chain	Residue
B	HOH562
B	HOH580
B	HOH620
B	HOH661
B	HOH665
B	HOH667
B	HOH669
B	HOH679
A	ASN194
A	HIS223
A	ILE226
A	ARG230
B	ILE16
B	ALA77
B	VAL78
B	GLY79
B	PRO81
B	ASP86
B	LEU94
B	ILE263
B	GLU282
B	HIS285
B	GLY286
B	SER287
B	ALA288
B	ASP290
B	ILE291
B	ALA297
B	ASN298
B	OXL402
B	NH4403
B	HOH509
B	HOH555

site_id	BC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE OXL B 402

Chain	Residue
A	LYS192
A	ASP225
A	MG405
B	ARG98
B	ARG108
B	ARG134
B	ASP250
B	NAI401
B	HOH659
B	HOH662
B	HOH702

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NH4 B 403

Chain	Residue
B	GLY76
B	GLU282
B	PRO283
B	HIS285
B	NAI401

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 404

Chain	Residue
B	ARG111
B	TRP304
B	LEU308
B	HIS324
B	LEU328
B	HOH644

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 405

Chain	Residue
B	THR152
B	GLU153
B	PRO215
B	HOH673

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 406

Chain	Residue
B	GLN234
B	ARG237
D	ARG7

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DTT B 407

Chain	Residue
B	ARG165
B	ARG206
B	HIS213
B	HOH538

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 401

Chain	Residue
C	ASP250
C	ASP254
C	OXL403
C	HOH521
C	HOH526
D	ASP225

site_id	BC9
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAI C 402

Chain	Residue
C	ILE16
C	ALA77
C	VAL78
C	GLY79
C	PRO81
C	ASP86
C	LEU94
C	GLU282
C	HIS285
C	GLY286
C	SER287
C	ALA288
C	ASP290
C	ILE291
C	ALA297
C	ASN298
C	OXL403
C	NH4404
C	HOH513
C	HOH532
C	HOH551
C	HOH574
C	HOH583
C	HOH588
C	HOH628
C	HOH677
D	ASN194
D	HIS223
D	ILE226
D	ARG230

site_id	CC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OXL C 403

Chain	Residue
C	ARG98
C	ARG108
C	ARG134
C	ASP250
C	MG401
C	NAI402
C	HOH678
D	LYS192
D	ASP225

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NH4 C 404

Chain	Residue
C	GLY76
C	GLU282
C	PRO283
C	HIS285
C	NAI402

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 405

Chain	Residue
C	ASP225
D	ASP250
D	OXL402
D	HOH705
D	HOH706

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 406

Chain	Residue
C	THR152
C	GLU153

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 407

Chain	Residue
C	LYS57
C	PRO60
C	ASP61

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 408

Chain	Residue
C	ARG111
C	TRP304
C	LEU308
C	HIS324
C	LEU328
C	HOH652

site_id	CC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DTT C 409

Chain	Residue
C	ILE226
C	LEU233
C	GLN234
D	THR262
D	ILE263
D	HOH685

site_id	CC8
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAI D 401

Chain	Residue
C	ASN194
C	HIS223
C	ILE226
C	ARG230
C	HOH623
D	ILE16
D	ALA77
D	VAL78
D	GLY79
D	PRO81
D	ASP86
D	LEU94
D	ILE263
D	GLU282
D	HIS285
D	GLY286
D	SER287
D	ALA288
D	ASP290
D	ILE291
D	ALA297
D	ASN298
D	OXL402
D	NH4403
D	HOH512
D	HOH515
D	HOH534
D	HOH594
D	HOH654
D	HOH707
D	HOH708

site_id	CC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OXL D 402

Chain	Residue
C	LYS192
C	ASP225
C	MG405
C	HOH535
D	ARG98
D	ARG108
D	ARG134
D	ASP250
D	NAI401
D	HOH764

site_id	DC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NH4 D 403

Chain	Residue
D	GLY76
D	GLU282
D	PRO283
D	HIS285
D	NAI401

site_id	DC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 404

Chain	Residue
D	LYS57
D	PRO60
D	ASP61
D	ASP62
D	HOH671
D	HOH680

site_id	DC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 405

Chain	Residue
D	ARG26
D	SER358
D	HOH557
D	HOH642
D	HOH675

site_id	DC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 406

Chain	Residue
D	ARG111
D	TRP304
D	LEU308
D	HIS324
D	LEU328
D	HOH748

site_id	DC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 407

Chain	Residue
C	ARG165
D	ASN151
D	HOH711

site_id	DC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DTT D 408

Chain	Residue
D	ASP14
D	GLY15
D	TRP80
D	PHE292
D	HOH632
D	HOH668
D	HOH738

Functional Information from PROSITE/UniProt

site_id	PS00470
Number of Residues	20
Details	IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLFGDIlSDlgPaca.GTIGI

Chain	Residue	Details
A	ASN246-ILE265

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P37412

Chain	Residue	Details
A	ASP225
D	ASP225
D	ILE251
D	LEU255
A	ILE251
A	LEU255
B	ASP225
B	ILE251
B	LEU255
C	ASP225
C	ILE251
C	LEU255

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1a05

Chain	Residue	Details
A	TYR141

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1a05

Chain	Residue	Details
B	TYR141

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1a05

Chain	Residue	Details
C	TYR141

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1a05

Chain	Residue	Details
D	TYR141

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1a05

Chain	Residue	Details
A	LYS192
A	ASP225

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1a05

Chain	Residue	Details
B	LYS192
B	ASP225

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1a05

Chain	Residue	Details
C	LYS192
C	ASP225

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1a05

Chain	Residue	Details
D	LYS192
D	ASP225

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