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Crystal structure of human junctional adhesion molecule type 1

Analyse Crystal structure of human junctional adhesion molecule type 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NBQ
Type: protein
Length: 417 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Junctional adhesion molecule 1
UniProt: Q9Y624
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Junctional adhesion molecule 1	protein	209	1% helix, 38% strand	Q9Y624
B	Junctional adhesion molecule 1	protein	208	1% helix, 38% strand	Q9Y624

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	63	0.37	0.79	25	empty

Interfaces

1 interface between chains.

A–B · 462 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1NBQ · Crystal Structure of Human Junctional Adhesion Molecule Type 1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y624 · AlphaFold monomer V2.0 prediction for junctional adhesion molecule a (Q9Y624) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9Y624
Elsewhere: RCSB PDB 1NBQ · PDBe 1NBQ · UniProt Q9Y624

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