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Crystal structure of DSCAM1 IG7 domain, isoform 9

Analyse Crystal structure of DSCAM1 IG7 domain, isoform 9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4X5L
Type: protein
Length: 384 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Down syndrome cell adhesion molecule, isoform am
UniProt: Q0E9K7
Ligands: NA
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Down syndrome cell adhesion molecule, isoform am	protein	96	0% helix, 51% strand	Q0E9K7

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains B, D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.28	0.75	17	empty

Interfaces

3 interfaces between chains.

B–D · 586 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 574 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 306 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4X5L · Crystal structure of Dscam1 Ig7 domain, isoform 9 · 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 Q0E9K7
Elsewhere: RCSB PDB 4X5L · PDBe 4X5L · UniProt Q0E9K7

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