Structure of PDB 1gvf Chain A

Receptor sequence
>1gvfA (length=273) Species: 562 (Escherichia coli) [Search protein sequence]
SIISTKYLLQDAQANGYAVPAFNIHNAETIQAILEVCSEMRSPVILAGTP
GTFKHIALEEIYALCSAYSTTYNMPLALHLDHHESLDDIRRKVHAGVRSA
MIDGSHFPFAENVKLVKSVVDFCHSQDCSVEAELGRLGSAFLTDPQEAKR
FVELTGVDSLAVAIGTAHGLYSKTPKIDFQRLAEIREVVDVPLVLHGASD
VPDEFVRRTIELGVTKVNVATELKIAFAGAVKAWFAENPQGNDPRYYMRV
GMDAMKEVVRNKINVCGSANRIS
3D structure
PDB1gvf Structure of Tagatose-1,6-Bisphosphate Aldolase; Insight Into Chiral Discrimination, Mechanism and Specificity of Class II Aldolases
ChainA
Resolution1.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D82 H83 H180 H208 N230
Catalytic site (residue number reindexed from 1) D81 H82 H168 H196 N218
Enzyme Commision number 4.1.2.40: tagatose-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 PGH A D82 H83 H180 G181 H208 G209 S211 N230 V231 A232 T233 D81 H82 H168 G169 H196 G197 S199 N218 V219 A220 T221
BS02 ZN A H83 H180 H208 H82 H168 H196
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0009025 tagatose-bisphosphate aldolase activity
GO:0016829 lyase activity
GO:0016832 aldehyde-lyase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0051289 protein homotetramerization
GO:2001059 D-tagatose 6-phosphate catabolic process
Cellular Component
GO:0005829 cytosol
GO:0032991 protein-containing complex
GO:1902494 catalytic complex

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Cellular Component
External links
PDB RCSB:1gvf, PDBe:1gvf, PDBj:1gvf
PDBsum1gvf
PubMed11940603
UniProtP0AB74|KBAY_ECOLI D-tagatose-1,6-bisphosphate aldolase subunit KbaY (Gene Name=kbaY)

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