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Crystal structure analysis of a human lysozyme mutant W64C C65A

Analyse Crystal structure analysis of a human lysozyme mutant W64C C65A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QSW
Type: protein
Length: 520 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Human lysozyme mutant
UniProt: P61626
Pockets: 7 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Human lysozyme mutant	protein	130	42% helix, 9% strand	P61626

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	295	0.72	0.85	36	empty
2	373	0.69	0.82	32	empty
3	120	0.51	0.82	35	empty
4	102	0.37	0.75	18	empty
5	93	0.37	0.75	14	empty

Interfaces

3 interfaces between chains.

B–C · 666 Å² buried · 8 hydrogen bonds · protein-protein
B–D · 469 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 404 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

1QSW · Crystal structure analysis of a human lysozyme mutant W64C C65A · 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 1QSW · PDBe 1QSW · UniProt P61626

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