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Crystal structure of anopholes gambiae odorant binding protein 20 in open state

Analyse Crystal structure of anopholes gambiae odorant binding protein 20 in open state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VB1
Type: protein
Length: 120 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AGAP005208-pa
UniProt: Q7Q9J3
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	AGAP005208-pa	protein	120	64% helix, 3% strand	Q7Q9J3

Ligands and binding sites

ACY · Acetic acid · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	214	0.69	0.86	31	empty

Modifications

Observed in the structure: 3 disulfide, 1 modified (disulfide, nonstandard).

Compared structures

3VB1 · Crystal Structure of Anopholes gambiae odorant binding protein 20 in open state · 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 Q7Q9J3
Elsewhere: RCSB PDB 3VB1 · PDBe 3VB1 · UniProt Q7Q9J3

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