MolNFT v1 · #66649 · protein

Crystal structure of T4 lysozyme with the unnatural amino acid P- acetyl-L-phenylalanine incorporated at position 131

3HWL: “Crystal structure of T4 lysozyme with the unnatural amino acid P- acetyl-L-phenylalanine incorporated at…”. X-ray diffraction, 3 ligands (4AF, CL, AZI), 1 pocket (best druggability 0.50). MolNFT v1 #66649 on GenesisL1: 3D structure…

PDB: 3HWL
Type: protein
Length: 161 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme
EC: 3.2.1.17
UniProt: P00720
Ligands: 4AF, CL, AZI
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme (EC 3.2.1.17)	protein	161	61% helix, 9% strand	P00720

Ligands and binding sites

4AF · 4-acetyl-L-phenylalanine · ligand · chains A
CL · Chloride ion · ion · 3 copies · chains A
AZI · Azide ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	210	0.50	0.76	27	empty

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

3HWL · Crystal Structure of T4 lysozyme with the unnatural amino acid p-Acetyl-L-Phenylalanine… · 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 P00720
Elsewhere: RCSB PDB 3HWL · PDBe 3HWL · UniProt P00720

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