MolNFT v1 · #49149 · protein

Crystal structure of putative secreted protein DUF305 from streptomyces coelicolor

2QF9: “Crystal structure of putative secreted protein DUF305 from streptomyces coelicolor”. X-ray diffraction, 2 pockets (best druggability 0.43). MolNFT v1 #49149 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2QF9
Type: protein
Length: 323 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative secreted protein
UniProt: Q8CK01
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative secreted protein	protein	162	73% helix, 0% strand	Q8CK01
B	Putative secreted protein	protein	161	75% helix, 0% strand	Q8CK01

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	79	0.43	0.80	18	empty
2	63	0.36	0.78	18	empty

Interfaces

1 interface between chains.

A–B · 1008 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 27 modified, 2 disulfide (engineered, disulfide).

Compared structures

2QF9 · Crystal structure of putative secreted protein DUF305 from Streptomyces coelicolor · 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 Q8CK01
Elsewhere: RCSB PDB 2QF9 · PDBe 2QF9 · UniProt Q8CK01

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