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Salivary protein from lutzomyia longipalpis. selenomethionine derivative

Analyse Salivary protein from lutzomyia longipalpis. selenomethionine derivative in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3Q6P
Type: protein
Length: 762 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 43.2 kda salivary protein
UniProt: Q5WPU9
Pockets: 6 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	43.2 kda salivary protein	protein	381	8% helix, 40% strand	Q5WPU9

Ligands and binding sites

CIT · Citric acid · additive · chains B

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

Pockets

6 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	1023	0.83	0.84	109	empty
2	542	0.79	0.85	66	empty
3	71	0.36	0.77	18	empty
4	53	0.32	0.77	16	empty
5	62	0.30	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 540 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 modified, 2 disulfide (engineered, disulfide).

Compared structures

3Q6P · Salivary protein from Lutzomyia longipalpis. Selenomethionine derivative · 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 Q5WPU9
Elsewhere: RCSB PDB 3Q6P · PDBe 3Q6P · UniProt Q5WPU9

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