Structure of PDB 5kmr Chain C

Receptor sequence

>5kmrC (length=391) Species: 986075 (Caldalkalibacillus thermarum TA2.A1)

KPSIVILGAGYGGIVAALGLQKRLNYNEADITLVNKNDYHYITTELHQPA
AGTMHHDQARVGIKELIDEKKIKFVKDTVVAIQQKVTLQNGELHYDYLVV
GLGSEPETFGIEGLREHAFSINSINSVRIIRQHIEYQFAKFAAEPERTDY
LTIVVGGAGFTGIEFVGELADRMPELCAEYDVDPKLVRIINVEAAPTVLP
GFDPALVNYAMDVLGGKGVEFKIGTPIKRCTPEGVVIEVDGEEEEIKAAT
VVWTGGVRGNSIVEKSGFETMRGRIKVDPYLRAPGHENIFIVGDCALIIN
EENNRPYPPTAQIAIQHGENVAANLAALIRGGSMTPFKPHIRGTVASLGR
NDAIGIVGGRKVYGHAASWLKKLIDMRYLYLIGGLSLVLKK

3D structure

• PDB: 5kmr The mechanism of catalysis by type-II NADH:quinone oxidoreductases.
• Chain: C
• Resolution: 3.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N127 F170 G206 V350 L353 K377
• Catalytic site (residue number reindexed from 1): N122 F165 G201 V345 L348 K372

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	C	G12 Y13 N37 K38 Y43 T45 T46 V81 L107 G108 D299 P314 T315 A316 Q317	G10 Y11 N35 K36 Y41 T43 T44 V79 L102 G103 D294 P309 T310 A311 Q312
BS02	NAD	C	F114 G162 F165 T166 V197 E198 A199 P205 I232 W258 G260 P314	F109 G157 F160 T161 V192 E193 A194 P200 I227 W253 G255 P309

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

External links

• PDB: RCSB:5kmr, PDBe:5kmr, PDBj:5kmr
• PDBsum: 5kmr
• PubMed: 28067272
• UniProt: F5L3B8