Structure of PDB 1z42 Chain B

Receptor sequence
>1z42B (length=337) Species: 1423 (Bacillus subtilis) [Search protein sequence]
ARKLFTPITIKDMTLKNRIVMSPMCMYSSHEKDGKLTPFHMAHYISRAIG
QVGLIIVEASAVNPQGRITDQDLGIWSDEHIEGFAKLTEQVKEQGSKIGI
QLAHAGRKAELEGDIFAPSAIAFDEQSATPVEMSAEKVKETVQEFKQAAA
RAKEAGFDVIEIHAAHGYLIHEFLSPLSNHRTDEYGGSPENRYRFLREII
DEVKQVWDGPLFVRVSASDYTDKGLDIADHIGFAKWMKEQGVDLIDCSSG
ALVHADINVFPGYQVSFAEKIREQADMATGAVGMITDGSMAEEILQNGRA
DLIFIGRELLRDPFFARTAAKQLNTEIPAPVQYERGW
3D structure
PDB1z42 The 1.3 A Crystal Structure of the Flavoprotein YqjM Reveals a Novel Class of Old Yellow Enzymes
ChainB
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C26 H164 H167 Y169 R215 D223
Catalytic site (residue number reindexed from 1) C25 H163 H166 Y168 R214 D222
Enzyme Commision number 1.6.99.1: NADPH dehydrogenase.
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 FMN B S23 P24 M25 C26 A60 Q102 H167 R215 V283 M285 G307 R308 S22 P23 M24 C25 A59 Q101 H166 R214 V282 M284 G306 R307
BS02 HBA B Y28 I69 H164 H167 Y169 Y27 I68 H163 H166 Y168
Gene Ontology
Molecular Function
GO:0003959 NADPH dehydrogenase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0009636 response to toxic substance

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Molecular Function
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Biological Process
External links
PDB RCSB:1z42, PDBe:1z42, PDBj:1z42
PDBsum1z42
PubMed15890652
UniProtP54550|NAMA_BACSU NADPH dehydrogenase (Gene Name=namA)

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