Structure of PDB 2npx Chain A

Receptor sequence

>2npxA (length=447) Species: 1351 (Enterococcus faecalis)

MKVIVLGSSHGGYEAVEELLNLHPDAEIQWYEKGDFISFLSCGMQLYLEG
KVKDVNSVRYMTGEKMESRGVNVFSNTEITAIQPKEHQVTVKDLVSGEER
VENYDKLIISPGAVPFELDIPGKDLDNIYLMRGRQWAIKLKQKTVDPEVN
NVVVIGSGYIGIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDVLTEE
MEANNITIATGETVERYEGDGRVQKVVTDKNAYDADLVVVAVGVRPNTAW
LKGTLELHPNGLIKTDEYMRTSEPDVFAVGDATLIKYNPADTEVNIALAT
NARKQGRFAVKNLEEPVKPFPGVQGSSGLAVFDYKFASTGINEVMAQKLG
KETKAVTVVEDYLMDFNPDKQKAWFKLVYDPETTQILGAQLMSKADLTAN
INAISLAIQAKMTIEDLAYADFFFQPAFDKPWNIINTAALEAVKQER

3D structure

• PDB: 2npx NADH binding site and catalysis of NADH peroxidase.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H10 I37 S41 C42 K139 Q142 K143 R303 F423
• Catalytic site (residue number reindexed from 1): H10 I37 S41 C42 K139 Q142 K143 R303 F423
• Enzyme Commision number: 1.11.1.1: NADH peroxidase.

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	L6 S9 H10 E32 K33 S41 C42 E78 I79 P111 G112 R132 I160 N247 G280 D281 A297 L298 A299	L6 S9 H10 E32 K33 S41 C42 E78 I79 P111 G112 R132 I160 N247 G280 D281 A297 L298 A299
BS02	NAD	A	G158 Y159 I160 D179 I180 Y188 V242 G243 A297	G158 Y159 I160 D179 I180 Y188 V242 G243 A297

Gene Ontology

Molecular Function

• GO:0004601 peroxidase activity
• GO:0016491 oxidoreductase activity
• GO:0016692 NADH peroxidase activity

Biological Process

• GO:0098869 cellular oxidant detoxification

External links

• PDB: RCSB:2npx, PDBe:2npx, PDBj:2npx
• PDBsum: 2npx
• PubMed: 8425532
• UniProt: P37062|NAPE_ENTFA NADH peroxidase (Gene Name=npr)