MolNFT v1 · #30335 · protein

Protein structure plasticity exemplified by insertion and deletion mutants in T4 lysozyme

210L: “Protein structure plasticity exemplified by insertion and deletion mutants in T4 lysozyme”. X-ray diffraction, 1 pocket (best druggability 0.53). MolNFT v1 #30335 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 210L
Type: protein
Length: 161 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T4 lysozyme
EC: 3.2.1.17
UniProt: P00720
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T4 lysozyme (EC 3.2.1.17)	protein	161	65% helix, 9% strand	P00720

Ligands and binding sites

HED · 2-hydroxyethyl disulfide · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	273	0.53	0.75	30	empty

Compared structures

210L · Protein structure plasticity exemplified by insertion and deletion mutants in 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 210L · PDBe 210L · UniProt P00720

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