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Structure of human PATCHED1

Analyse Structure of human PATCHED1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6OEU
Type: protein
Length: 964 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein patched homolog 1
UniProt: Q13635
Ligands: NAG
Pockets: 15 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 52% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein patched homolog 1	protein	964	52% helix, 5% strand	Q13635

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A

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

Pockets

15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	962	0.88	0.89	95	empty
2	690	0.80	0.84	62	empty
3	66	0.70	0.96	25	empty
4	137	0.61	0.85	27	empty
5	201	0.59	0.81	32	empty

Modifications

Observed in the structure: 1 glycan (N-glycosylation).

Compared structures

6OEU · Structure of human Patched1 · the same entry in another collection · chain A against A, TM-score 1.00
Q13635 · AlphaFold monomer V2.0 prediction for protein patched homolog 1 (Q13635) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q13635
Elsewhere: RCSB PDB 6OEU · PDBe 6OEU · UniProt Q13635

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