The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in escherichia coli by a cDNA constructed from its rat homologue. Determined by X-ray diffraction at 2.5 Å resolution. Released 31 Aug 1994.
Explore 1HDR in 3D Show helices and sheets RCSB PDB PDBe
1HDR contains 13 α-helices and 14 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-15 | 5 | 1 |
| α-helix | 20-31 | 12 | |
| β-strand | 35-40 | 6 | 1 |
| β-strand | 45 | 1 | 2 |
| β-strand | 47 | 1 | 2 |
| β-strand | 49-52 | 4 | 1 |
| α-helix | 53-54 | 2 | |
| α-helix | 59-74 | 16 | |
| β-strand | 79-84 | 6 | 1 |
| β-strand | 92 | 1 | 3 |
| α-helix | 99-106 | 8 | |
| α-helix | 107-112 | 6 | |
| α-helix | 113-124 | 12 | |
| β-strand | 125-134 | 10 | 1 |
| α-helix | 137-140 | 4 | |
| β-strand | 146 | 1 | 3 |
| α-helix | 147-164 | 18 | |
| β-strand | 175-180 | 6 | 1 |
| β-strand | 184 | 1 | 4 |
| α-helix | 187-190 | 4 | |
| α-helix | 198-200 | 3 | |
| β-strand | 202 | 1 | 4 |
| α-helix | 203 | 1 | |
| α-helix | 204-215 | 12 | |
| α-helix | 220-222 | 3 | |
| β-strand | 226-232 | 7 | 1 |
| β-strand | 235-241 | 7 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dihydropteridine reductase | A | protein | 244 | Homo sapiens | P09417 (AlphaFold model) |
>1HDR_1 DIHYDROPTERIDINE REDUCTASE (chains A) MAAAAAAGEARRVLVYGGRGALGSRCVQAFRARNWWVASVDVVENEEASASIIVKMTDSF TEQADQVTAEVGKLLGEEKVDAILCVAGGWAGGNAKSKSLFKNCDLMWKQSIWTSTISSH LATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNSGMPPGAAAIAV LPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQVVTTEGRTELT PAYF
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAD | Nicotinamide-adenine-dinucleotide | C21 H27 N7 O14 P2 | 1 |
The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue. Su, Y., Varughese, K.I., Xuong, N.H. et al. J Biol Chem (1993) 268:26836-26841. PubMed
Other PDB entries of the same protein (UniProt P09417 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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