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Crystal structure of cross-linked mvins R77C trimer at 1.9A resolution

Analyse Crystal structure of cross-linked mvins R77C trimer at 1.9A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XU6
Type: protein
Length: 189 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: A1T557
Ligands: TDA
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	189	68% helix, 6% strand	A1T557

Ligands and binding sites

TDA · N-tridecanoic acid · ligand · 2 copies · chains A
BOG · octyl beta-D-glucopyranoside · additive · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	221	0.76	0.90	35	TDA
2	68	0.30	0.73	13	empty

Compared structures

4XU6 · Crystal structure of cross-linked MvINS R77C trimer at 1.9A resolution · the same entry in another collection · chain A against A, TM-score 1.00
A1T557 · AlphaFold monomer V2.0 prediction for insig protein homolog (A1T557) · a predicted model of the same protein · 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 A1T557
Elsewhere: RCSB PDB 4XU6 · PDBe 4XU6 · UniProt A1T557

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