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Crystal structure and ligand binding studies of a screened peptide complexed with streptavidin

Analyse Crystal structure and ligand binding studies of a screened peptide complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PTS
Type: protein
Length: 234 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin; Peptide (fshpqnt)
UniProt: P22629
Pockets: 2 · best druggability 0.48

Structure

x-ray diffraction · 3 distinct chains · 9% helix, 59% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Streptavidin	protein	119	8% helix, 58% strand	P22629
B	Streptavidin	protein	112	9% helix, 61% strand	P22629
P	Peptide (fshpqnt)	protein	3	0% helix, 0% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	97	0.48	0.80	17	empty
2	51	0.29	0.76	21	empty

Interfaces

2 interfaces between chains.

A–B · 1595 Å² buried · 23 hydrogen bonds · protein-protein
B–P · 122 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1PTS · Crystal structure and ligand binding studies of a screened peptide complexed with… · 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 P22629
Elsewhere: RCSB PDB 1PTS · PDBe 1PTS · UniProt P22629

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