Structure of PDB 1uxv Chain A

Receptor sequence

>1uxvA (length=499) Species: 2271 (Thermoproteus tenax) [Search protein sequence]

AGLLEGVIKEKGGVPVYPSYLAGEWGGSGQEIEVKSPIDLATIAKVISPS
REEVERTLDVLFKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLV
MNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGL
VRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAM
AVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVV
KVGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKL
VLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAI
EDAVEKGGRVLAGGRRLGPTYVQPTLVEAPADRVKDMVLYKREVFAPVAL
AVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDM
PRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVFNYKGKGVWKYE

3D structure

PDB

1uxv Structural Basis of Allosteric Regulation and Substrate Specificity of the Non-Phosphorylating Glyceraldehyde 3-Phosphate Dehydrogenase from Thermoproteus Tenax

Chain

Resolution

2.35 Å

3D
structure

Catalytic site residues are labeled in the structure
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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)(+)].

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	NAP	A	I164 T165 F167 N168 K191 S193 I194 P223 G224 E228 T242 G243 S244 V247 E263 L264 G265 C297 E395 F397	I162 T163 F165 N166 K189 S191 I192 P221 G222 E226 T240 G241 S242 V245 E261 L262 G263 C295 E393 F395
BS02	AMP	A	R72 K132 I133 G134 R154 R155	R70 K130 I131 G132 R152 R153

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

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