Structure of PDB 1nhr Chain A

Receptor sequence
>1nhrA (length=447) Species: 1351 (Enterococcus faecalis) [Search protein sequence]
MKVIVLGSSHGGYEAVEELLNLHPDAEIQWYEKGDFISFCSCGMQLYLEG
KVKDVNSVRYMTGEKMESRGVNVFSNTEITAIQPKEHQVTVKDLVSGEER
VENYDKLIISPGAVPFELDIPGKDLDNIYLMRGRQWAIKLKQKTVDPEVN
NVVVIGSGYIGIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDVLTEE
MEANNITIATGETVERYEGDGRVQKVVTDKNAYDADLVVVAVGVRPNTAW
LKGTLELHPNGLIKTDEYMRTSEPDVFAVGDATLIKYNPADTEVNIALAT
NARKQGRFAVKNLEEPVKPFPGVQGSSGLAVFDYKFASTGINEVMAQKLG
KETKAVTVVEDYLMDFNPDKQKAWFKLVYDPETTQILGAQLMSKADLTAN
INAISLAIQAKMTIEDLAYADFFFQPAFDKPWNIINTAALEAVKQER
3D structure
PDB1nhr An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 I79 S110 P111 G112 R132 I160 N247 G280 D281 A297 L298 A299 L6 S9 H10 E32 K33 S41 I79 S110 P111 G112 R132 I160 N247 G280 D281 A297 L298 A299
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016491 oxidoreductase activity
GO:0016692 NADH peroxidase activity
Biological Process
GO:0098869 cellular oxidant detoxification

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Molecular Function
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Biological Process
External links
PDB RCSB:1nhr, PDBe:1nhr, PDBj:1nhr
PDBsum1nhr
PubMed7711038
UniProtP37062|NAPE_ENTFA NADH peroxidase (Gene Name=npr)

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