Structure of PDB 5kmr Chain A

Receptor sequence

>5kmrA (length=393) Species: 986075 (Caldalkalibacillus thermarum TA2.A1)

KPSIVILGAGYGGIVAALGLQKRLNYNEADITLVNKNDYHYITTELHQPA
AGTMHHDQARVGIKELIDEKKIKFVKDTVVAIDREQQKVTLQNGELHYDY
LVVGLGSEPETFGIEGLREHAFSINSINSVRIIRQHIEYQFAKFAAEPER
TDYLTIVVGGAGFTGIEFVGELADRMPELCAEYDVDPKLVRIINVEAAPT
VLPGFDPALVNYAMDVLGGKGVEFKIGTPIKRCTPEGVVIEVDGEEEEIK
AATVVWTGGVRGNSIVEKSGFETMRGRIKVDPYLRAPGHENIFIVGDCAL
IINEENNRPYPPTAQIAIQHGENVAANLAALIRGGSMTPFKPHIRGTVAS
LGRNDAIGIVGGRKVYGHAASWLKKLIDMRYLYLIGGLSLVLK

3D structure

• PDB: 5kmr The mechanism of catalysis by type-II NADH:quinone oxidoreductases.
• Chain: A
• 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): N125 F168 G204 V348 L351 K375

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	G12 Y13 N37 K38 T45 T46 H49 V81 L107 G108 G298 D299 P314 T315 A316 Q317	G10 Y11 N35 K36 T43 T44 H47 V79 L105 G106 G296 D297 P312 T313 A314 Q315
BS02	NAD	A	G162 F165 T166 V197 E198 A199 P205 I232 W258 G260 P314 V350	G160 F163 T164 V195 E196 A197 P203 I230 W256 G258 P312 V348

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