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Characterization of peptide ligands against WDR5 isolated using phage display technique

Analyse Characterization of peptide ligands against WDR5 isolated using phage display… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DNO
Type: protein
Length: 618 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Wd repeat-containing protein 5; Cys-arg-thr-leu-pro-phe
UniProt: P61964
Pockets: 6 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Wd repeat-containing protein 5	protein	303	0% helix, 51% strand	P61964
C, D	Cys-arg-thr-leu-pro-phe	protein	6	0% helix, 0% strand	—

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	817	0.84	0.86	68	empty
2	478	0.73	0.82	44	empty
3	198	0.57	0.80	30	empty
4	66	0.54	0.87	19	empty
5	60	0.42	0.81	17	empty

Interfaces

3 interfaces between chains.

A–B · 544 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 507 Å² buried · 5 hydrogen bonds · protein-protein
B–D · 499 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7DNO · Characterization of Peptide Ligands Against WDR5 Isolated Using Phage Display Technique · 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 P61964
Elsewhere: RCSB PDB 7DNO · PDBe 7DNO · UniProt P61964

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