MolNFT v1 · #43592 · protein

Crystal structures of the apo-and holomutant human lysozymes with an introduced CA2+ binding site

2LHM: “Crystal structures of the apo-and holomutant human lysozymes with an introduced CA2+ binding site”. X-ray diffraction, 1 pocket (best druggability 0.34). MolNFT v1 #43592 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2LHM
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 0.34

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Human lysozyme (EC 3.2.1.17)	protein	130	39% 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	76	0.34	0.75	14	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

2LHM · Crystal structures of the apo-and holomutant human lysozymes with an introduced CA2+… · 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 2LHM · PDBe 2LHM · UniProt P61626

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