Structure of PDB 1h62 Chain A

Receptor sequence
>1h62A (length=364) Species: 550 (Enterobacter cloacae) [Search protein sequence]
SAEKLFTPLKVGAVTAPNRVFMAPLTRLRSIEPGDIPTPLMGEYYRQRAS
AGLIISEATQISAQAKGYAGAPGLHSPEQIAAWKKITAGVHAEDGRIAVQ
LWHTGRISHSSIQPGGQAPVSASALNANTRTSLRDENGNAIRVDTTTPRA
LELDEIPGIVNDFRQAVANAREAGFDLVELHSAHGYLLHQFLSPSSNQRT
DQYGGSVENRARLVLEVVDAVCNEWSADRIGIRVSPIGTFQNVDNGPNEE
ADALYLIEELAKRGIAYLHMSETDLAGGKPYSEAFRQKVRERFHGVIIGA
GAYTAEKAEDLIGKGLIDAVAFGRDYIANPDLVARLQKKAELNPQRPESF
YGGGAEGYTDYPSL
3D structure
PDB1h62 Crystal Structure of Pentaerythritol Tetranitrate Reductase: "Flipped" Binding Geometries for Steroid Substrates in Different Redox States of the Enzyme
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T26 H181 H184 Y186 R233 Q241
Catalytic site (residue number reindexed from 1) T26 H181 H184 Y186 R233 Q241
Enzyme Commision number ?
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 ANB A T26 Y68 S132 R142 H181 H184 Y186 Q241 Y351 T26 Y68 S132 R142 H181 H184 Y186 Q241 Y351 MOAD: Kd=17uM
PDBbind-CN: -logKd/Ki=4.77,Kd=17uM
BS02 FMN A P24 L25 T26 A58 Q100 H181 H184 R233 A302 G323 R324 Y351 P24 L25 T26 A58 Q100 H181 H184 R233 A302 G323 R324 Y351
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:1h62, PDBe:1h62, PDBj:1h62
PDBsum1h62
PubMed11428899
UniProtP71278

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