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Crystal structure of streptavidin with one wild type subunit and three mutated subunits (N23A/S27D/S45A)

Analyse Crystal structure of streptavidin with one wild type subunit and three mutated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TO2
Type: protein
Length: 482 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Streptavidin	protein	121	2% helix, 55% strand	P22629
D	Streptavidin	protein	119	5% helix, 56% strand	P22629

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · chains A, D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	736	0.75	0.80	102	PEG
2	432	0.65	0.78	50	empty
3	337	0.64	0.79	41	empty

Interfaces

6 interfaces between chains.

A–B · 1606 Å² buried · 28 hydrogen bonds · protein-protein
C–D · 1589 Å² buried · 28 hydrogen bonds · protein-protein
A–D · 486 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 411 Å² buried · 2 hydrogen bonds · protein-protein
A–C · 209 Å² buried · 4 hydrogen bonds · protein-protein

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 5TO2 · PDBe 5TO2 · UniProt P22629

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