Structure of PDB 3hml Chain B

Receptor sequence
>3hmlB (length=236) Species: 272620 (Klebsiella pneumoniae subsp. pneumoniae MGH 78578) [Search protein sequence]
ITDTLSPQAFEEALRAKGDFYHIHHPYHIAMHNGNATREQIQGWVANRFY
YQTTIPLKDAAIMANCPDAQTRRKWVQRILDHDGSDGGIEAWLRLGEAVG
LSRDDLLSERHVLPGVRFAVDAYLNFARRACWQEAACSSLTELFAPSWPQ
HYPWIKEEGYFYFRSRLSDVEHGLALAKAYCDSAEKQNRMLEILQFKLDI
LWSMLDAMTMAYALQRPPYHTVTDKAAWHTTRLVLE
3D structure
PDB3hml Structural studies of mutant forms of the PQQ-forming enzyme PqqC in the presence of product and substrate
ChainB
Resolution2.35 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.3.3.11: pyrroloquinoline-quinone synthase.
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 PQQ B Y23 H24 R50 Y53 Y128 S144 T146 K214 Y21 H22 R48 Y51 Y123 S139 T141 K197
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0033732 pyrroloquinoline-quinone synthase activity
Biological Process
GO:0006790 sulfur compound metabolic process
GO:0018189 pyrroloquinoline quinone biosynthetic process
GO:0044281 small molecule metabolic process
GO:1901615 organic hydroxy compound metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3hml, PDBe:3hml, PDBj:3hml
PDBsum3hml
PubMed20602352
UniProtA6T9H1|PQQC_KLEP7 Pyrroloquinoline-quinone synthase (Gene Name=pqqC)

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