4AOU - JenaLib

Title :   CTIDH BOUND TO NADP. THE COMPLEX STRUCTURES OF ISOCITRATE DEHYDROGENASE FROM CLOSTRIDIUM THERMOCELLUM AND DESULFOTALEA PSYCHROPHILA, SUPPORT A NEW ACTIVE SITE LOCKING MECHANISM

Authors :   H. -K. S. Leiros, A. -E. Fedoy, I. Leiros, I. H. Steen

Date :   30 Mar 12 (Deposition) - 11 Jul 12 (Release) - 22 May 13 (Revision)

Method :   X-RAY DIFFRACTION

Resolution :   2.50

Chains :   Asym. Unit : A
Biol. Unit 1: A  (2x)

Keywords :   Oxidoreductase, Temperature Adaptation, Thermophilic, Psychrophilic, Nadp+ Selectivity, Domain Movements (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )

Reference :   H. -K. S. Leiros, A. -E. Fedoy, I. Leiros, I. H. Steen
The Complex Structures Of Isocitrate Dehydrogenase From Clostridium Thermocellum And Desulfotalea Psychrophila Suggest A New Active Site Locking Mechanism
Febs Open Bio. V. 2 159 2012
PubMed-ID: 23650595 | Reference-DOI: 10.1016/J.FOB.2012.06.003

Compounds

Structural Features

Chains, Units

Ligands, Modified Residues, Ions (3, 3)

Sites (3, 3)

SS Bonds (0, 0)

Cis Peptide Bonds (0, 0)

Sequence-Structure Mapping

SAPs(SNPs)/Variants (0, 0)

PROSITE Motifs (0, 0)

Exons (0, 0)

Sequences/Alignments

Asymmetric Unit

Reformat:	Number of residues per line = ('0' or empty: single-line sequence representation)
	Number of residues per labelling interval =
	UniProt sequence: complete aligned part

Show mapping:	SCOP domains	CATH domains	Pfam domains	Secondary structure (by author)
	SAPs(SNPs)	PROSITE motifs	Exons
	(details for a mapped element are shown in a popup box when the mouse pointer rests over it)

Chain A from PDB  Type:PROTEIN  Length:401
 aligned with A3DC45_CLOTH | A3DC45 from UniProtKB/TrEMBL  Length:402

    Alignment length:401
                                    11        21        31        41        51        61        71        81        91       101       111       121       131       141       151       161       171       181       191       201       211       221       231       241       251       261       271       281       291       301       311       321       331       341       351       361       371       381       391       401 
         A3DC45_CLOTH     2 SKIKMKVPLVEMDGDEMTRIIWRLIKENLLEPYIELNTEYYDLGLENRDKTEDQVTIDAARAIQKYGVGVKCATITPNAQRVEEYNLKKMWKSPNGTIRAILDGTVFRAPIVVNSIKPFVKGWKKPISIARHAYGDVYKNVEYYVPSAGKAELVFTSENGEVSRQTIHEFDGPGVIMGMHNTDKSIRSFARACFNYALDMNQDLWFSTKDTISKTYDHRFKDIFQEIYENEYKEKFEAKNLQYFYTLIDDAVARIIRSEGGMVWACKNYDGDVMSDMVASAFGSLAMMTSVLVSPDGKYEFEAAHGTVTRHYYKHLKGEETSTNSMATIFAWTGALKKRGELDGIKELVDFATKLEQASVQTIENGVMTKDLASLSEVPEKKIVNTEDFLKEIRKTFEGMA 402
               SCOP domains d4aoua_ A: automated matches                                                                                                                                                                                                                                                                                                                                                                                      SCOP domains
               CATH domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ........eeeee.hhhhhhhhhhhhhhhh.......eeeee.hhhhhhhh.hhhhhhhhhhhhhhheeee......hhhhhhhhh......hhhhhhhhhhh.eeeeee.................eeeee..hhhhhheeeee...eeeeeeee.....eeeeeeeee...eeeee...hhhhhhhhhhhhhhhhhhhh..eeeee......hhhhhhhhhhhhhhhh.hhhhhhhh...eeeeehhhhhhhhhhh....eeeehhhhhhhhhhhhhhhhh....eeeeee.....eeeee....hhhhhhhhhh.......hhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhh.eehhhhhh.......ee.hhhhhhhhhhhhhhh.. Sec.struct. author
                 SAPs(SNPs) ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 4aou A   2 SKIKMKVPLVEMDGDEMTRIIWRLIKENLLEPYIELNTEYYDLGLENRDKTEDQVTIDAARAIQKYGVGVKCATITPNAQRVEEYNLKKMWKSPNGTIRAILDGTVFRAPIVVNSIKPFVKGWKKPISIARHAYGDVYKNVEYYVPSAGKAELVFTSENGEVSRQTIHEFDGPGVIMGMHNTDKSIRSFARACFNYALDMNQDLWFSTKDTISKTYDHRFKDIFQEIYENEYKEKFEAKNLQYFYTLIDDAVARIIRSEGGMVWACKNYDGDVMSDMVASAFGSLAMMTSVLVSPDGKYEFEAAHGTVTRHYYKHLKGEETSTNSMATIFAWTGALKKRGELDGIKELVDFATKLEQASVQTIENGVMTKDLASLSEVPEKKIVNTEDFLKEIRKTFEGMA 402
                                    11        21        31        41        51        61        71        81        91       101       111       121       131       141       151       161       171       181       191       201       211       221       231       241       251       261       271       281       291       301       311       321       331       341       351       361       371       381       391       401

Legend:		→ Mismatch	(orange background)
	-	→ Gap	(green background, '-', border residues have a numbering label)
		→ Modified Residue	(blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
	x	→ Chemical Group	(purple background, 'x', labelled with number + name, e.g. ACE or NH2)
	extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '\|'

Classification and Annotation

SCOP Domains (1, 1)

CATH Domains (0, 0)

Pfam Domains (0, 0)

Gene Ontology (10, 10)

Asymmetric Unit(hide GO term definitions)

Chain A (A3DC45_CLOTH | A3DC45)

molecular function
	GO:0051287	NAD binding	Interacting selectively and non-covalently with nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
	GO:0004450	isocitrate dehydrogenase (NADP+) activity	Catalysis of the reaction: isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+.
	GO:0000287	magnesium ion binding	Interacting selectively and non-covalently with magnesium (Mg) ions.
	GO:0046872	metal ion binding	Interacting selectively and non-covalently with any metal ion.
	GO:0000166	nucleotide binding	Interacting selectively and non-covalently with a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
	GO:0016491	oxidoreductase activity	Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
	GO:0016616	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor	Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
biological process
	GO:0006102	isocitrate metabolic process	The chemical reactions and pathways involving isocitrate, the anion of isocitric acid, 1-hydroxy-1,2,3-propanetricarboxylic acid. Isocitrate is an important intermediate in the TCA cycle and the glycoxylate cycle.
	GO:0055114	oxidation-reduction process	A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.
	GO:0006099	tricarboxylic acid cycle	A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

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	4aou
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