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Streptavidin-2-iminobiotin complex, pH 3.25, space group I222, crystallized from 4.3 M ammonium sulfate

Analyse Streptavidin-2-iminobiotin complex, pH 3.25, space group I222, crystallized… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RTQ
Type: protein
Length: 244 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Ligands: IMI
Pockets: 4 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Streptavidin	protein	123	8% helix, 58% strand	P22629
D	Streptavidin	protein	121	5% helix, 56% strand	P22629

Ligands and binding sites

IMI · 2-iminobiotin · ligand · 2 copies · chains B, D

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

Pockets

4 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	89	0.45	0.80	18	IMI
2	81	0.44	0.80	17	IMI
3	71	0.35	0.76	23	empty
4	72	0.34	0.76	21	empty

Interfaces

1 interface between chains.

B–D · 1584 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

2RTQ · Streptavidin-2-iminobiotin complex, pH 3.25, space group I222, crystallized from 4.3 M… · the same entry in another collection · chain B against B, 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 2RTQ · PDBe 2RTQ · UniProt P22629

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