Structure of PDB 5wed Chain B

Receptor sequence
>5wedB (length=394) Species: 986075 (Caldalkalibacillus thermarum TA2.A1) [Search protein sequence]
KPSIVILGAGYGGIVAALGLQKRLNYNEADITLVNKNDYHYITTELHQPA
AGTMHHDQARVGIKELIDEKKIKFVKDTVVAIDREQQKVTLQNGELHYDY
LVVGLGSEPETFGIEGLREHAFSINSINSVRIIRQHIEYQFAKFAAEPER
TDYLTIVVGGAGFTGIEFVGELADRMPELCAEYDVDPKLVRIINVEAAPT
VLPGFDPALVNYAMDVLGGKGVEFKIGTPIKRCTPEGVVIEVDGEEEEIK
AATVVWTGGVRGNSIVEKSGFETMRGRIKVDPYLRAPGHENIFIVGDCAL
IINEENNRPYPPTAQIAIQHGENVAANLAALIRGGSMTPFKPHIRGTVAS
LGRNDAIGIVGGRKVYGHAASWLKKLIDMRYLYLIGGLSLVLKK
3D structure
PDB5wed Crystal structure of type II NADH:quinone oxidoreductase from Caldalkalibacillus thermarum with an improved resolution of 2.15 angstrom.
ChainB
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N127 F170 G206 V350 L353 K377
Catalytic site (residue number reindexed from 1) N125 F168 G204 V348 L351 K375
Enzyme Commision number ?
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 B G12 Y13 N37 K38 Y43 T45 T46 H49 V81 L107 T166 G298 D299 P314 T315 A316 Q317 G10 Y11 N35 K36 Y41 T43 T44 H47 V79 L105 T164 G296 D297 P312 T313 A314 Q315
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003955 NAD(P)H dehydrogenase (quinone) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0019646 aerobic electron transport chain

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Molecular Function
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Biological Process
External links
PDB RCSB:5wed, PDBe:5wed, PDBj:5wed
PDBsum5wed
PubMed28994401
UniProtF5L3B8

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