Structure of PDB 5kmr Chain D

Receptor sequence
>5kmrD (length=394) Species: 986075 (Caldalkalibacillus thermarum TA2.A1) [Search protein sequence]
KPSIVILGAGYGGIVAALGLQKRLNYNEADITLVNKNDYHYITTELHQPA
AGTMHHDQARVGIKELIDEKKIKFVKDTVVAIDREQQKVTLQNGELHYDY
LVVGLGSEPETFGIEGLREHAFSINSINSVRIIRQHIEYQFAKFAAEPER
TDYLTIVVGGAGFTGIEFVGELADRMPELCAEYDVDPKLVRIINVEAAPT
VLPGFDPALVNYAMDVLGGKGVEFKIGTPIKRCTPEGVVIEVDGEEEEIK
AATVVWTGGVRGNSIVEKSGFETMRGRIKVDPYLRAPGHENIFIVGDCAL
IINEENNRPYPPTAQIAIQHGENVAANLAALIRGGSMTPFKPHIRGTVAS
LGRNDAIGIVGGRKVYGHAASWLKKLIDMRYLYLIGGLSLVLKK
3D structure
PDB5kmr The mechanism of catalysis by type-II NADH:quinone oxidoreductases.
ChainD
Resolution3.0 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 D G12 Y13 N37 K38 Y43 T45 T46 H49 V81 L107 G108 D299 P314 T315 A316 G10 Y11 N35 K36 Y41 T43 T44 H47 V79 L105 G106 D297 P312 T313 A314
BS02 NAD D F114 G162 G164 F165 T166 E198 A199 P205 W258 G260 P314 F112 G160 G162 F163 T164 E196 A197 P203 W256 G258 P312
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
View graph for
Biological Process
External links
PDB RCSB:5kmr, PDBe:5kmr, PDBj:5kmr
PDBsum5kmr
PubMed28067272
UniProtF5L3B8

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