MolNFT v1 · #944 · protein

Lysozyme from bacteriophage lambda

1AM7: “Lysozyme from bacteriophage lambda”. X-ray diffraction, 6 pockets (best druggability 0.68). MolNFT v1 #944 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1AM7
Type: protein
Length: 462 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme
EC: 3.2.1.17
UniProt: P03706
Pockets: 6 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Lysozyme (EC 3.2.1.17)	protein	154	43% helix, 8% strand	P03706

Ligands and binding sites

IPA · Isopropyl alcohol · additive · 3 copies · chains A, B, C

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	360	0.68	0.81	50	empty
2	318	0.67	0.82	46	IPA
3	127	0.44	0.77	17	empty
4	138	0.43	0.75	25	IPA
5	110	0.41	0.76	17	empty

Interfaces

2 interfaces between chains.

B–C · 912 Å² buried · 16 hydrogen bonds · protein-protein
A–C · 886 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (nonstandard).

Compared structures

1AM7 · Lysozyme from bacteriophage lambda · 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 P03706
Elsewhere: RCSB PDB 1AM7 · PDBe 1AM7 · UniProt P03706

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