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Structural basis for dscam isoform specificity

Analyse Structural basis for dscam isoform specificity in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2V5R
Type: protein
Length: 782 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dscam
UniProt: Q9NBA1
Ligands: NAG
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dscam	protein	391	4% helix, 42% strand	Q9NBA1

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains B, A

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	974	0.79	0.81	93	GOL
2	65	0.54	0.87	18	empty
3	63	0.52	0.86	17	empty
4	57	0.36	0.78	14	empty
5	52	0.33	0.77	17	empty

Interfaces

1 interface between chains.

A–B · 437 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

2V5R · Structural basis for Dscam isoform specificity · 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 Q9NBA1
Elsewhere: RCSB PDB 2V5R · PDBe 2V5R · UniProt Q9NBA1

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