MolNFT v1 · #30442 · protein

Structural characterisation of an engineered tandem repeat contrasts the importance of context and sequence in protein folding

262L · Lysozyme: “Structural characterisation of an engineered tandem repeat contrasts the importance of context and sequence…”. X-ray diffraction, 3 pockets (best druggability 0.48). MolNFT v1 #30442 on GenesisL1: 3D structure, binding…

PDB: 262L
Type: protein
Length: 346 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme
EC: 3.2.1.17
UniProt: P00720
Pockets: 3 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lysozyme (EC 3.2.1.17)	protein	173	63% helix, 10% strand	P00720

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	232	0.48	0.74	26	empty
2	77	0.39	0.78	15	empty
3	69	0.31	0.74	11	empty

Compared structures

262L · Structural characterisation of an engineered tandem repeat contrasts the importance of… · 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 P00720
Elsewhere: RCSB PDB 262L · PDBe 262L · UniProt P00720

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