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Crystal structure of bacteriophage P22 lysozyme mutant L87M

Analyse Crystal structure of bacteriophage P22 lysozyme mutant L87M in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ANX
Type: protein
Length: 292 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme
EC: 3.2.1.17
UniProt: P09963
Ligands: SM, MG, IOD, SO4
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lysozyme (EC 3.2.1.17)	protein	146	55% helix, 11% strand	P09963

Ligands and binding sites

SM · Samarium (III) ion · metal · 3 copies · chains A, B
MG · Magnesium ion · metal · chains A
IOD · Iodide ion · ion · 8 copies · chains A, B
SO4 · Sulfate ion · ion · 6 copies · chains A, B

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

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	177	0.51	0.78	29	IOD
2	68	0.42	0.81	23	SO4
3	61	0.27	0.73	14	SO4

Interfaces

1 interface between chains.

A–B · 593 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2ANX · crystal structure of bacteriophage P22 lysozyme mutant L87M · 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 P09963
Elsewhere: RCSB PDB 2ANX · PDBe 2ANX · UniProt P09963

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