MolNFT v1 · #50775 · protein

Streptavidin-glycoluril complex, pH 2.50, space group I222

2RTH: “Streptavidin-glycoluril complex, pH 2.50, space group I222”. X-ray diffraction, 1 ligand (GLL), 3 pockets (best druggability 0.45). MolNFT v1 #50775 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2RTH
Type: protein
Length: 244 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Ligands: GLL
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Streptavidin	protein	123	8% helix, 55% strand	P22629
D	Streptavidin	protein	121	7% helix, 55% strand	P22629

Ligands and binding sites

GLL · Glycoluril · ligand · 2 copies · chains B, D
ACT · Acetate ion · additive · 2 copies · chains B, 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	80	0.45	0.80	17	ACT, GLL
2	81	0.43	0.79	17	ACT, GLL
3	66	0.31	0.75	21	empty

Interfaces

1 interface between chains.

B–D · 1582 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

2RTH · Streptavidin-glycoluril complex, pH 2.50, space group I222 · 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 2RTH · PDBe 2RTH · UniProt P22629

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