Structure of PDB 1bhy Chain A

Receptor sequence
>1bhyA (length=482) Species: 487 (Neisseria meningitidis) [Search protein sequence]
GSADAEYDVVVLGGGPGGYSAAFAAADEGLKVAIVERYKTLGGVCLNVGC
IPSKALLHNAAVIDEVRHLAANGIKYPEPELDIDMLRAYKDGVVSRLTGG
LAGMAKSRKVDVIQGDGQFLDPHHLEVSLTAGDAYEQAAPTGEKKIVAFK
NCIIAAGSRVTKLPFIPEDPRIIDSSGALALKEVPGKLLIIGGGIIGLEM
GTVYSTLGSRLDVVEMMDGLMQGADRDLVKVWQKQNEYRFDNIMVNTKTV
AVEPKEDGVYVTFEGANAPKEPQRYDAVLVAAGRAPNGKLISAEKAGVAV
TDRGFIEVDKQMRTNVPHIYAIGDIVGQPMLAHKAVHEGHVAAENCAGHK
AYFDARVIPGVAYTSPEVAWVGETELSAKASARKITKANFPWAASGRAIA
NGCDKPFTKLIFDAETGRIIGGGIVGPNGGDMIGEVYLAIEMGCDAADIG
KTIHPHPTLGESIGMAAEVALGTCTDLPPQKK
3D structure
PDB1bhy Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values.
ChainA
Resolution4.18 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L157 C161 C166 S169 I311 E315 H570 H572 E577 P595 Q596
Catalytic site (residue number reindexed from 1) L41 C45 C50 S53 I195 E199 H454 H456 E461 P479 Q480
Enzyme Commision number 1.8.1.4: dihydrolipoyl 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 FAD A L128 P132 G133 E152 R153 Y154 G159 V160 C161 G165 C166 K170 D232 G233 Y251 A272 G273 D440 L447 A448 L12 P16 G17 E36 R37 Y38 G43 V44 C45 G49 C50 K54 D116 G117 Y135 A156 G157 D324 L331 A332
Gene Ontology
Molecular Function
GO:0004148 dihydrolipoyl dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
GO:0050660 flavin adenine dinucleotide binding

View graph for
Molecular Function
External links
PDB RCSB:1bhy, PDBe:1bhy, PDBj:1bhy
PDBsum1bhy
PubMed10089406
UniProtQ51225

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