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Crystal structure of the patched-1 (PTCH1) ectodomain 1

Analyse Crystal structure of the patched-1 (PTCH1) ectodomain 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6RTX
Type: protein
Length: 267 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein patched homolog 1
UniProt: Q13635
Ligands: NAG
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein patched homolog 1	protein	267	36% helix, 18% strand	Q13635

Ligands and binding sites

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

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.63	0.87	18	empty
2	131	0.44	0.76	23	empty
3	98	0.35	0.75	17	empty

Modifications

Observed in the structure: 3 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

6RTX · Crystal structure of the Patched-1 (PTCH1) ectodomain 1 · 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 6RTX · PDBe 6RTX · UniProt Q13635

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