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Miniprotein mp-1 complex with streptavidin

Analyse Miniprotein mp-1 complex with streptavidin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HY2
Type: protein
Length: 540 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin; Mp-1
UniProt: P22629
Pockets: 4 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Streptavidin	protein	123	11% helix, 54% strand	P22629
E, F, G, H	Mp-1	protein	12	25% helix, 0% strand	—

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	459	0.70	0.81	58	empty
2	469	0.66	0.79	58	empty
3	171	0.42	0.73	31	empty
4	132	0.37	0.73	28	empty

Interfaces

14 interfaces between chains.

C–D · 1622 Å² buried · 26 hydrogen bonds · protein-protein
A–B · 1589 Å² buried · 22 hydrogen bonds · protein-protein
D–H · 522 Å² buried · 4 hydrogen bonds · protein-protein
C–G · 459 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 430 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

1HY2 · Miniprotein mp-1 complex with streptavidin · 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 1HY2 · PDBe 1HY2 · UniProt P22629

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