MolNFT v1 · #13366 · protein

Perturbation of TRP 138 in T4 lysozyme by mutations at gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties

1L98: “Perturbation of TRP 138 in T4 lysozyme by mutations at gln 105 used to correlate changes in structure…”. X-ray diffraction, 1 pocket (best druggability 0.51). MolNFT v1 #13366 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1L98
Type: protein
Length: 164 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 0.51

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T4 lysozyme (EC 3.2.1.17)	protein	164	64% helix, 9% strand	P00720

Ligands and binding sites

BME · Beta-mercaptoethanol · additive · 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	253	0.51	0.75	28	empty

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

1L98 · Perturbation of TRP 138 in T4 lysozyme by mutations at gln 105 used to correlate changes… · 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 1L98 · PDBe 1L98 · UniProt P00720

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