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Apo-core-streptavidin at pH 7.5

Analyse Apo-core-streptavidin at pH 7.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SWB
Type: protein
Length: 465 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Streptavidin	protein	120	5% helix, 57% strand	P22629
B, C, D	Streptavidin	protein	115	8% helix, 58% strand	P22629

Pockets

4 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	334	0.69	0.82	48	empty
2	358	0.62	0.78	40	empty
3	358	0.61	0.77	47	empty
4	308	0.60	0.78	42	empty

Interfaces

6 interfaces between chains.

C–D · 1638 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1622 Å² buried · 19 hydrogen bonds · protein-protein
A–D · 444 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 387 Å² buried · 3 hydrogen bonds · protein-protein
B–D · 197 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

1SWB · Apo-core-streptavidin at pH 7.5 · 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 1SWB · PDBe 1SWB · UniProt P22629

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