Structure of PDB 1cru Chain B

Receptor sequence

>1cruB (length=452) Species: 471 (Acinetobacter calcoaceticus)

DVPLTPSQFAKAKSENFDKKVILSNLNKPHALLWGPDNQIWLTERATGKI
LRVNPESGSVKTVFQVPEIVNDADGQNGLLGFAFHPDFKNNPYIYISGTF
KNPKSTDKELPNQTIIRRYTYNKSTDTLEKPVDLLAGLPSSKDHQSGRLV
IGPDQKIYYTIGDQGRNQLAYLFLPNQAQHTPTQQELNGKDYHTYMGKVL
RLNLDGSIPKDNPSFNGVVSHIYTLGHRNPQGLAFTPNGKLLQSEQGPNS
DDEINLIVKGGNYGWPNVAGYKDDSGYAYANYSAAANKSIKDLAQNGVKV
AAGVPVTKESEWTGKNFVPPLKTLYTVQDTYNYNDPTCGEMTYICWPTVA
PSSAYVYKGGKKAITGWENTLLVPSLKRGVIFRIKLDPTYSTTYDDAVPM
FKSNNRYRDVIASPDGNVLYVLTDTAGNVQKDDGSVTNTLENPGSLIKFT
YK

3D structure

• PDB: 1cru Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complex.
• Chain: B
• Resolution: 1.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H144 D163 R228 A269 Y271 D273 E309
• Catalytic site (residue number reindexed from 1): H144 D163 R228 A269 Y271 D273 E309
• 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	B	E253 Y263	E253 Y263
BS02	CA	B	A269 Y271 D273 E309	A269 Y271 D273 E309
BS03	CA	B	G247 P248	G247 P248
BS04	PQQ	B	Q76 H144 R228 N229 Q246 Y343 T348 A350 L376 K377 R406 R408	Q76 H144 R228 N229 Q246 Y343 T348 A350 L376 K377 R406 R408

Gene Ontology

Molecular Function

• GO:0008876 quinoprotein glucose dehydrogenase activity
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding

External links

• PDB: RCSB:1cru, PDBe:1cru, PDBj:1cru
• PDBsum: 1cru
• PubMed: 10518528
• UniProt: P13650|DHGB_ACICA Quinoprotein glucose dehydrogenase B (Gene Name=gdhB)