MolNFT v1 · #176611 · protein
The crystal structure of human spr from biortus.
7DSF · Sepiapterin reductase: “The crystal structure of human spr from biortus.”. X-ray diffraction, 2 ligands (NAP, ZN), 3 pockets (best druggability 0.76). MolNFT v1 #176611 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7DSF
- Type
- protein
- Length
- 518 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sepiapterin reductase
- EC
- 1.1.1.153
- UniProt
- P35270
- Ligands
- NAP, ZN
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sepiapterin reductase (EC 1.1.1.153) | protein | 261 | 48% helix, 17% strand | P35270 |
| B | Sepiapterin reductase (EC 1.1.1.153) | protein | 257 | 48% helix, 18% strand | P35270 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 554 | 0.76 | 0.83 | 66 | NAP, ACT |
| 2 | 524 | 0.75 | 0.83 | 62 | NAP, ACT |
| 3 | 76 | 0.35 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1928 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P35270
- Elsewhere: RCSB PDB 7DSF · PDBe 7DSF · UniProt P35270
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