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Structure of a lysozyme Fab complex

Analyse Structure of a lysozyme Fab complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TSA
Type: protein
Length: 486 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme C; Fab heavy chain; Fab light chain
EC: 3.2.1.17
UniProt: P00698
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 3 distinct chains · 14% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme C (EC 3.2.1.17)	protein	68	56% helix, 3% strand	P00698
H	Fab heavy chain	protein	208	7% helix, 50% strand	—
L	Fab light chain	protein	210	6% helix, 49% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	562	0.61	0.74	54	empty
2	90	0.39	0.77	17	empty
3	74	0.33	0.76	26	empty

Interfaces

3 interfaces between chains.

H–L · 1608 Å² buried · 17 hydrogen bonds · protein-protein
A–H · 457 Å² buried · 8 hydrogen bonds · protein-protein
A–L · 373 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

4TSA · Structure of a lysozyme FAb complex · 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 P00698
Elsewhere: RCSB PDB 4TSA · PDBe 4TSA · UniProt P00698

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