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Dissection of the functional role of structural elements of tyrosine- 63 in the catalytic action of human lysozyme

Analyse Dissection of the functional role of structural elements of tyrosine- 63 in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TCY
Type: protein
Length: 130 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Human lysozyme
EC: 3.2.1.17
UniProt: P61626
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Human lysozyme (EC 3.2.1.17)	protein	130	38% helix, 12% strand	P61626

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.30	0.75	13	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1TCY · Dissection of the functional role of structural elements of tyrosine-63 in the catalytic… · 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 P61626
Elsewhere: RCSB PDB 1TCY · PDBe 1TCY · UniProt P61626

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