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Crystal structure of gadolinium derivative of hewl solved using intense free-electron laser radiation

Analyse Crystal structure of gadolinium derivative of hewl solved using intense… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5C6L
Type: protein
Length: 129 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme C
EC: 3.2.1.17
UniProt: P00698
Ligands: DO3, GD, CL
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme C (EC 3.2.1.17)	protein	129	40% helix, 11% strand	P00698

Ligands and binding sites

DO3 · 10-((2R)-2-hydroxypropyl)-1,4,7,10-tetraazacyclododecane 1,4,7-triacetic acid · ligand · 2 copies · chains A
GD · Gadolinium atom · metal · 2 copies
CL · Chloride ion · ion · 4 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.31	0.75	15	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5C6L · Crystal Structure of Gadolinium derivative of HEWL solved using intense Free-Electron… · 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 5C6L · PDBe 5C6L · UniProt P00698

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