MolNFT v1 · #30319 · protein

How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme

201L: “How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme”. X-ray diffraction, 3 pockets (best druggability 0.68). MolNFT v1 #30319 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 201L
Type: protein
Length: 330 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T4 lysozyme
EC: 3.2.1.17
UniProt: P00720
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T4 lysozyme (EC 3.2.1.17)	protein	164	63% helix, 9% strand	P00720
B	T4 lysozyme (EC 3.2.1.17)	protein	166	62% helix, 9% strand	P00720

Ligands and binding sites

BME · Beta-mercaptoethanol · additive · 2 copies · chains B

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

Pockets

3 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	814	0.68	0.75	50	empty
2	286	0.60	0.79	39	empty
3	66	0.34	0.77	15	empty

Interfaces

1 interface between chains.

A–B · 544 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

201L · How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme · 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 201L · PDBe 201L · UniProt P00720

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