Structure of PDB 1hdr Chain A

Receptor sequence
>1hdrA (length=236) Species: 9606 (Homo sapiens) [Search protein sequence]
EARRVLVYGGRGALGSRCVQAFRARNWWVASVDVVENEEASASIIVKMTD
SFTEQADQVTAEVGKLLGEEKVDAILCVAGGWAGGNAKSKSLFKNCDLMW
KQSIWTSTISSHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVH
QLCQSLAGKNSGMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFL
VETFHDWITGKNRPSSGSLIQVVTTEGRTELTPAYF
3D structure
PDB1hdr The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y149 K153
Catalytic site (residue number reindexed from 1) Y142 K146
Enzyme Commision number 1.5.1.34: 6,7-dihydropteridine reductase.
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 NAD A G16 R18 G19 A20 L21 D40 V53 V85 A86 G87 T113 Y149 K153 P181 V182 T183 L184 G9 R11 G12 A13 L14 D33 V46 V78 A79 G80 T106 Y142 K146 P174 V175 T176 L177 MOAD: Kd=0.034uM
Gene Ontology
Molecular Function
GO:0004155 6,7-dihydropteridine reductase activity
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0070402 NADPH binding
GO:0070404 NADH binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0006559 L-phenylalanine catabolic process
GO:0006729 tetrahydrobiopterin biosynthetic process
GO:0051066 dihydrobiopterin metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1hdr, PDBe:1hdr, PDBj:1hdr
PDBsum1hdr
PubMed8262916
UniProtP09417|DHPR_HUMAN Dihydropteridine reductase (Gene Name=QDPR)

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