MolNFT v1 · #14140 · protein

Structural changes of the active site cleft and different saccharide binding modes in human lysozyme co-crystallized with hexa-N-acetyl- chitohexaose at pH 4.0

1LZR: “Structural changes of the active site cleft and different saccharide binding modes in human lysozyme…”. X-ray diffraction, 2 ligands (NAG, CL), 1 pocket (best druggability 0.35). MolNFT v1 #14140 on GenesisL1: 3D structure, binding…

PDB: 1LZR
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: P00695
Ligands: NAG, CL
Pockets: 1 · best druggability 0.35

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	P00695

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
CL · Chloride ion · ion · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	77	0.35	0.75	16	NAG

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1LZR · Structural changes of the active site cleft and different saccharide binding modes in… · 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 P00695
Elsewhere: RCSB PDB 1LZR · PDBe 1LZR · UniProt P00695

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