Structure of PDB 3hrd Chain B

Receptor sequence
>3hrdB (length=330) Species: 1528 (Eubacterium barkeri) [Search protein sequence]
MKKRGKGVGSMWYGIGNTGLPNPAAAFVEIHGDGSANVMFGAADIGQGSG
TAMAQIAAEELGLDYEKIHVTWGDTMVTPDGGATSASRQTLITGNAVILA
CRQAKETLAKTAAEKLDCAPEELSFRDNTVFITADPERSMTYGELMAAMK
AAGRMAVGAGSYNPNTTGLAPENMSGIPFEVYSYATTIAEVEVDTETGEV
DVLKVVSAHDVGTPINRSMVEGQIEGGVTMGQGFVLMEEIEVNTKNGAIK
NPSMSKYIIPSNRDVPEIHSILVESEGGPGPFGAKGVGEPALIPMIPAVV
AAIEDALGTRFTHTPIMPKDIVAAVKAQEK
3D structure
PDB3hrd The Mo-Se active site of nicotinate dehydrogenase
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) E289 P290
Catalytic site (residue number reindexed from 1) E289 P290
Enzyme Commision number 1.17.1.5: nicotinate dehydrogenase.
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 MCN B I45 G46 Q47 G48 S49 S85 S87 Q89 T90 I215 N216 M219 V220 Q223 K285 G286 V287 G288 E289 I45 G46 Q47 G48 S49 S85 S87 Q89 T90 I215 N216 M219 V220 Q223 K285 G286 V287 G288 E289
BS02 NIO B N17 T18 N17 T18
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050138 nicotinate dehydrogenase activity
Biological Process
GO:1901848 nicotinate catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3hrd, PDBe:3hrd, PDBj:3hrd
PDBsum3hrd
PubMed19549881
UniProtQ0QLF1|NDMMS_EUBBA Nicotinate dehydrogenase medium molybdopterin subunit (Gene Name=ndhM)

[Back to BioLiP]