MolNFT v1 · #17283 · protein

Structural genomics of caenorhabditis elegans : dihydropteridine reductase

1OOE: “Structural genomics of caenorhabditis elegans : dihydropteridine reductase”. X-ray diffraction, 3 pockets (best druggability 0.62). MolNFT v1 #17283 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1OOE
Type: protein
Length: 470 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydropteridine reductase
EC: 1.6.99.7
UniProt: Q9XVJ3
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dihydropteridine reductase (EC 1.6.99.7)	protein	235	43% helix, 24% strand	Q9XVJ3

Ligands and binding sites

MES · 2-(N-morpholino)-ethanesulfonic acid · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	381	0.62	0.77	42	empty
2	385	0.61	0.77	43	empty
3	179	0.46	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 1538 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

1OOE · Structural Genomics of Caenorhabditis elegans : Dihydropteridine reductase · the same entry in another collection · chain A against A, TM-score 1.00

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 Q9XVJ3
Elsewhere: RCSB PDB 1OOE · PDBe 1OOE · UniProt Q9XVJ3

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