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T4 lysozyme mutant with cys 54 replaced by thr, cys 97 replaced by ala, thr 21 replaced by cys and lys 124 replaced by cys (C54T,C97A, T21C,K124C)

Analyse T4 lysozyme mutant with cys 54 replaced by thr, cys 97 replaced by ala, thr 21… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1B6I
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (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	Protein (lysozyme) (EC 3.2.1.17)	protein	162	65% helix, 9% strand	P00720

Ligands and binding sites

HED · 2-hydroxyethyl disulfide · 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	256	0.53	0.76	30	empty

Compared structures

1B6I · T4 lysozyme mutant with cys 54 replaced by thr, cys 97 replaced by ala, thr 21 replaced… · 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 1B6I · PDBe 1B6I · UniProt P00720

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