Research workbench

Crystal structure of the SPYTAG/SPYCATCHER complex

Analyse Crystal structure of the SPYTAG/SPYCATCHER complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MLI
Type: protein
Length: 189 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fibronectin binding protein; Spytag
UniProt: Q8G9G1
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 3 distinct chains · 0% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fibronectin binding protein	protein	82	0% helix, 52% strand	Q8G9G1
C	Fibronectin binding protein	protein	83	0% helix, 52% strand	Q8G9G1
B, D	Spytag	protein	12	0% helix, 50% strand	—

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	175	0.49	0.77	40	empty

Interfaces

3 interfaces between chains.

A–B · 893 Å² buried · 15 hydrogen bonds · protein-protein
C–D · 890 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 495 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 isopeptide (isopeptide).

Compared structures

4MLI · Crystal structure of the SpyTag/SpyCatcher complex · 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 Q8G9G1
Elsewhere: RCSB PDB 4MLI · PDBe 4MLI · UniProt Q8G9G1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.