Structure of PDB 1rvg Chain A

Receptor sequence
>1rvgA (length=299) Species: 271 (Thermus aquaticus) [Search protein sequence]
MLVTGLEILKKAREEGYGVGAFNVNNMEFLQAVLEAAEEQRSPVILALSE
GAMKYGGRALTLMAVELAKEARVPVAVHLDHGSSYESVLRALRAGFTSVM
IDKSHEDFETNVRETRRVVEAAHAVGVTVEAELGRLAGIEEKDALLTNPE
EARIFMERTGADYLAVAIGTSHGAYKGKGRPFIDHARLERIARLVPAPLV
LHGASAVPPELVERFRASGGEIGEAAGIHPEDIKKAISLGIAKINTDTDL
RLAFTALIREALNKNPKEFDPRKYLGPAREAVKEVVKSRMELFGSVGRA
3D structure
PDB1rvg Induced Fit Movements and Metal Cofactor Selectivity of Class II Aldolases: STRUCTURE OF THERMUS AQUATICUS FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D80 H81 E140 H178 H208 N251
Catalytic site (residue number reindexed from 1) D80 H81 E140 H172 H202 N245
Enzyme Commision number 4.1.2.13: fructose-bisphosphate aldolase.
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 SO4 A H178 G179 G209 S211 D253 T254 H172 G173 G203 S205 D247 T248
BS02 SO4 A S104 R135 S104 R135
BS03 CO A H81 H178 H208 H81 H172 H202
BS04 CO A H81 H178 H208 H81 H172 H202
Gene Ontology
Molecular Function
GO:0004332 fructose-bisphosphate aldolase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0016832 aldehyde-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006096 glycolytic process
GO:0030388 fructose 1,6-bisphosphate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1rvg, PDBe:1rvg, PDBj:1rvg
PDBsum1rvg
PubMed14699122
UniProtQ9RHA2

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