Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2GUG

NAD-dependent formate dehydrogenase from Pseudomonas sp.101 in complex with formate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0008863	molecular_function	formate dehydrogenase (NAD+) 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	0032787	biological_process	monocarboxylic acid metabolic process
A	0042183	biological_process	formate catabolic process
A	0051287	molecular_function	NAD binding
B	0005737	cellular_component	cytoplasm
B	0008863	molecular_function	formate dehydrogenase (NAD+) 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	0032787	biological_process	monocarboxylic acid metabolic process
B	0042183	biological_process	formate catabolic process
B	0051287	molecular_function	NAD binding
C	0005737	cellular_component	cytoplasm
C	0008863	molecular_function	formate dehydrogenase (NAD+) 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	0032787	biological_process	monocarboxylic acid metabolic process
C	0042183	biological_process	formate catabolic process
C	0051287	molecular_function	NAD binding
D	0005737	cellular_component	cytoplasm
D	0008863	molecular_function	formate dehydrogenase (NAD+) 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	0032787	biological_process	monocarboxylic acid metabolic process
D	0042183	biological_process	formate catabolic process
D	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 A 478

Chain	Residue
A	SER184
A	PEG480
A	HOH526
C	ASP13
C	THR18
C	TYR19

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 D 480

Chain	Residue
D	GLU298
D	TYR326
D	HOH550
B	THR18
D	SER184
D	HIS185

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 479

Chain	Residue
A	PRO97
A	PHE98
A	GLY121
A	ILE122
A	ASN146
A	PEG476
A	HOH587

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT B 401

Chain	Residue
B	PRO97
B	PHE98
B	ILE122
B	ASN146
B	HOH499

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT C 401

Chain	Residue
C	PRO97
C	PHE98
C	GLY121
C	ILE122
C	ASN146
C	HOH531

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PEG A 476

Chain	Residue
A	ILE122
A	ASN146
A	SER147
A	VAL150
A	ILE202
A	THR282
A	FMT479
A	HOH554

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PEG A 477

Chain	Residue
A	PRO31
A	TYR144
A	ARG201
A	ALA205
A	ARG208
A	ARG209
C	GLU190
C	ASP214

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG A 480

Chain	Residue
A	GLU298
A	TYR326
A	PG4478

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG B 481

Chain	Residue
B	LEU204

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG C 482

Chain	Residue
C	ALA199
C	GLY200

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG C 483

Chain	Residue
C	GLU298
C	TYR326

Functional Information from PROSITE/UniProt

site_id	PS00065
Number of Residues	28
Details	D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGTVAaGRIGlavlrrlapfdvh.LHyTD

Chain	Residue	Details
A	VAL194-ASP221

site_id	PS00670
Number of Residues	23
Details	D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MYpvCDVVtLNcPlhpeTehMiN

Chain	Residue	Details
A	MET244-ASN266

site_id	PS00671
Number of Residues	17
Details	D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. FKrGaYIVNtARGkLCD

Chain	Residue	Details
A	PHE273-ASP289

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2006","firstPage":"627","lastPage":"631","volume":"51","journal":"Crystallogr. Rep.","title":"Crystal structure of the complex of NAD-dependent formate dehydrogenase from methylotrophic bacterium Pseudomonas sp.101 with formate.","authors":["Filippova E.V.","Polyakov K.M.","Tikhonova T.V.","Stekhanova T.N.","Boiko K.M.","Sadihov I.G.","Tishkov V.I.","Labrou N.","Popov V.O."],"citationCrossReferences":[{"database":"DOI","id":"10.1134/S1063774506040146"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8114093","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8114093","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 2nac

Chain	Residue	Details
A	GLN313
A	HIS332
A	ASN146
A	ARG284

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 2nac

Chain	Residue	Details
B	GLN313
B	HIS332
B	ASN146
B	ARG284

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 2nac

Chain	Residue	Details
C	GLN313
C	HIS332
C	ASN146
C	ARG284

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 2nac

Chain	Residue	Details
D	GLN313
D	HIS332
D	ASN146
D	ARG284

site_id	MCSA1
Number of Residues	4
Details	M-CSA 902

Chain	Residue	Details
A	ASN146	electrostatic stabiliser
A	ARG284	electrostatic stabiliser
A	GLN313	modifies pKa
A	HIS332	enhance reactivity

site_id	MCSA2
Number of Residues	4
Details	M-CSA 902

Chain	Residue	Details
B	ASN146	electrostatic stabiliser
B	ARG284	electrostatic stabiliser
B	GLN313	modifies pKa
B	HIS332	enhance reactivity

site_id	MCSA3
Number of Residues	4
Details	M-CSA 902

Chain	Residue	Details
C	ASN146	electrostatic stabiliser
C	ARG284	electrostatic stabiliser
C	GLN313	modifies pKa
C	HIS332	enhance reactivity

site_id	MCSA4
Number of Residues	4
Details	M-CSA 902

Chain	Residue	Details
D	ASN146	electrostatic stabiliser
D	ARG284	electrostatic stabiliser
D	GLN313	modifies pKa
D	HIS332	enhance reactivity

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