MolNFT v1 · #122310 · protein

Crystal structure of DEG9

5IL9 · Protease do-like 9: “Crystal structure of DEG9”. X-ray diffraction, 7 pockets (best druggability 0.75). MolNFT v1 #122310 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5IL9
Type: protein
Length: 920 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease do-like 9
EC: 3.4.21.-
UniProt: Q9FL12
Pockets: 7 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protease do-like 9 (EC 3.4.21.-)	protein	465	20% helix, 37% strand	Q9FL12
B	Protease do-like 9 (EC 3.4.21.-)	protein	455	20% helix, 36% strand	Q9FL12

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 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	1121	0.75	0.78	103	empty
2	527	0.63	0.75	63	empty
3	194	0.49	0.76	26	empty
4	107	0.43	0.78	22	empty
5	113	0.39	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 1529 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

5IL9 · Crystal structure of Deg9 · the same entry in another collection · chain A against A, TM-score 1.00
Q9FL12 · AlphaFold monomer V2.0 prediction for protease do-like 9 (Q9FL12) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9FL12
Elsewhere: RCSB PDB 5IL9 · PDBe 5IL9 · UniProt Q9FL12

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