Structure of PDB 1uxr Chain A Binding Site BS02

Receptor Information

>1uxr Chain A (length=499) Species: 2271 (Thermoproteus tenax) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

AGLLEGVIKEKGGVPVYPSYLAGEWGGSGQEIEVKSPIDLATIAKVISPS
REEVERTLDVLFKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLV
MNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGL
VRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAM
AVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVV
KVGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKL
VLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAI
EDAVEKGGRVLAGGRRLGPTYVQPTFVEAPADRVKDMVLYKREVFAPVAL
AVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDM
PRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVFNYKGKGVWKYE

Ligand information

Ligand ID

F6P

InChI

InChI=1S/C6H13O9P/c7-2-6(10)5(9)4(8)3(15-6)1-14-16(11,12)13/h3-5,7-10H,1-2H2,(H2,11,12,13)/t3-,4-,5+,6-/m1/s1

InChIKey

BGWGXPAPYGQALX-ARQDHWQXSA-N

SMILES

Software	SMILES
ACDLabs 10.04	O=P(O)(O)OCC1OC(O)(CO)C(O)C1O
OpenEye OEToolkits 1.5.0	C(C1C(C(C(O1)(CO)O)O)O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0	C([C@@H]1[C@H]([C@@H]([C@](O1)(CO)O)O)O)OP(=O)(O)O
CACTVS 3.341	OC[C]1(O)O[CH](CO[P](O)(O)=O)[CH](O)[CH]1O
CACTVS 3.341	OC[C@@]1(O)O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@@H]1O

Formula

C6 H13 O9 P

Name

6-O-phosphono-beta-D-fructofuranose;
FRUCTOSE-6-PHOSPHATE;
6-O-phosphono-beta-D-fructose;
6-O-phosphono-D-fructose;
6-O-phosphono-fructose

PDB chain

1uxr Chain A Residue 1503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1uxr Structural Basis of Allosteric Regulation and Substrate Specificity of the Non-Phosphorylating Glyceraldehyde 3-Phosphate Dehydrogenase from Thermoproteus Tenax
Resolution	2.3 Å
Binding residue (original residue number in PDB)	R72 R79 I133 R154
Binding residue (residue number reindexed from 1)	R70 R77 I131 R152
Annotation score	1

Enzymatic activity

Catalytic site (original residue number in PDB)	N168 K191 E263 C297 E395 E473
Catalytic site (residue number reindexed from 1)	N166 K189 E261 C295 E393 E471
Enzyme Commision number	1.2.1.90: glyceraldehyde-3-phosphate dehydrogenase [NAD(P)(+)].

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0008886	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity
GO:0008911	lactaldehyde dehydrogenase (NAD+) activity
GO:0016491	oxidoreductase activity
GO:0016620	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0043878	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
GO:0050661	NADP binding
GO:0051287	NAD binding

View graph for
Molecular Function

External links

PDB	RCSB:1uxr, PDBe:1uxr, PDBj:1uxr
PDBsum	1uxr
PubMed	15288789
UniProt	O57693\|GAPN_THETE NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase (Gene Name=gapN)

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