Structure of PDB 1qbi Chain A

Receptor sequence
>1qbiA (length=434) Species: 471 (Acinetobacter calcoaceticus) [Search protein sequence]
DVPLTPSQFAKAKSENFDKKVILSNLNKPHALLWGPDNQIWLTERATGKI
LRVNPESGSVKTVFQVPEIVNDADGQNGLLGFAFHPDFKNNPYIYISGTF
KNPKPNQTIIRRYTYNKSTDTLEKPVDLLAGLPSSKDHQSGRLVIGPDQK
IYYTIGDQGRNQLAYLFLPNQAQHTPTQQELNGKDYHTYMGKVLRLNLDG
SIPKDNPSFNGVVSHIYTLGHRNPQGLAFTPNGKLLQSEQGPNSDDEINL
IVKGGNYGWPNVAGYKDDSGYAYANYSAAANKSIKDLAQNGVKVAAGVPV
TKESEWTGKNFVPPLKTLYTVQDTYNYNCWPTVAPSSAYVYKGGKKAITG
WENTLLVPSLKRGVIFRIKLDPTYSTTYDDAVPMFKSNNRYRDVIASPDG
NVLYVLTDTAGNVQKDDGSVTNTLENPGSLIKFT
3D structure
PDB1qbi The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat.
ChainA
Resolution1.72 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H144 D163 R228 A269 Y271 D273 E309
Catalytic site (residue number reindexed from 1) H138 D157 R222 A263 Y265 D267 E303
Enzyme Commision number 1.1.5.2: quinoprotein glucose dehydrogenase (PQQ, quinone).
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 CA A A269 Y271 D273 E309 A263 Y265 D267 E303
BS02 CA A E253 Y263 E247 Y257
BS03 CA A G247 P248 G241 P242
Gene Ontology
Molecular Function
GO:0008876 quinoprotein glucose dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:1qbi, PDBe:1qbi, PDBj:1qbi
PDBsum1qbi
PubMed10366508
UniProtP13650|DHGB_ACICA Quinoprotein glucose dehydrogenase B (Gene Name=gdhB)

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