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G129A human lysozyme

Analyse G129A human lysozyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IP7
Type: protein
Length: 260 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.9
Source: Homo sapiens
Molecule: Lysozyme C
EC: 3.2.1.17
UniProt: P61626
Ligands: NA
Pockets: 3 · best druggability 0.48

Structure

x-ray diffraction · resolution 1.9 · 1 distinct chain · 39% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lysozyme C (EC 3.2.1.17)	protein	130	39% helix, 12% strand	P61626

Ligands and binding sites

NA · Sodium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	131	0.48	0.79	21	empty
2	148	0.42	0.75	20	empty
3	58	0.32	0.76	13	empty

Interfaces

1 interface between chains.

A–B · 535 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

1IP7 · G129A human lysozyme · the same entry in another collection · chain A against A, TM-score 1.00
P61626 · AlphaFold monomer V2.0 prediction for lysozyme C (P61626) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 1IP7 · PDBe 1IP7 · UniProt P61626

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