Structure of PDB 1rv8 Chain A

Receptor sequence
>1rv8A (length=297) Species: 271 (Thermus aquaticus) [Search protein sequence]
MLVTGLEILKKAREEGYGVGAFNVNNMEFLQAVLEAAEEQRSPVILALSE
GAMKYGGRALTLMAVELAKEARVPVAVHLDHGSSYESVLRALRAGFTSVM
IDKSHEDFETNVRETRRVVEAAHAVGVTVEAELGRLAGIKDALLTNPEEA
RIFMERTGADYLAVAIGTSHGAYKGKGRPFIDHARLERIARLVPAPLVLH
GASAVPPELVERFRASGGEIGEAAGIHPEDIKKAISLGIAKINTDTDLRL
AFTALIREALNKNPKEFDPRKYLGPAREAVKEVVKSRMELFGSVGRA
3D structure
PDB1rv8 Induced Fit Movements and Metal Cofactor Selectivity of Class II Aldolases: STRUCTURE OF THERMUS AQUATICUS FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE.
ChainA
Resolution2.3 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 H178 H208 N251
Catalytic site (residue number reindexed from 1) D80 H81 H170 H200 N243
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 G179 K182 G209 S211 D253 T254 G171 K174 G201 S203 D245 T246
BS02 SO4 A R116 H123 R116 H123
BS03 CO A H81 H178 H208 H81 H170 H200
BS04 CO A H81 L136 H178 H208 H81 L136 H170 H200
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:1rv8, PDBe:1rv8, PDBj:1rv8
PDBsum1rv8
PubMed14699122
UniProtQ9RHA2

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