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Crystal structure of streptavidin mutant (M3) a combination of M1+M2

Analyse Crystal structure of streptavidin mutant (M3) a combination of M1+M2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RXK
Type: protein
Length: 244 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Ligands: BNI
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Streptavidin	protein	120	8% helix, 57% strand	P22629
B	Streptavidin	protein	124	8% helix, 54% strand	P22629

Ligands and binding sites

BNI · 5-(2-oxo-hexahydro-thieno[3,4-d]imidazol-6-yl)-pentanoic acid (4-nitro-phenyl)-amide · ligand · 2 copies · chains A, B

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

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	75	0.37	0.76	14	BNI
2	55	0.31	0.75	13	BNI

Interfaces

1 interface between chains.

A–B · 1593 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

1RXK · crystal structure of streptavidin mutant (M3) a combination of M1+M2 · 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 1RXK · PDBe 1RXK · UniProt P22629

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