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Crystal structure of streptavidin mutant L124R (M1) complexed with biotinyl P-nitroanilide (bni)

Analyse Crystal structure of streptavidin mutant L124R (M1) complexed with biotinyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RXH
Type: protein
Length: 239 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Ligands: BNI
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Streptavidin	protein	118	3% helix, 55% strand	P22629
B	Streptavidin	protein	121	3% helix, 55% 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

3 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	91	0.47	0.80	18	BNI
2	99	0.45	0.79	18	BNI
3	59	0.28	0.75	24	empty

Interfaces

1 interface between chains.

A–B · 1626 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

1RXH · Crystal structure of streptavidin mutant L124R (M1) complexed with biotinyl… · 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 1RXH · PDBe 1RXH · UniProt P22629

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