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C-terminal domain of endolysin from phage CD27L is a trigger and release factor

Analyse C-terminal domain of endolysin from phage CD27L is a trigger and release factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4CU5
Type: protein
Length: 510 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endolysin
UniProt: B6SBV8
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Endolysin	protein	85	41% helix, 26% strand	B6SBV8

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	1065	0.70	0.75	81	empty
2	73	0.36	0.77	13	empty
3	90	0.35	0.74	16	empty

Interfaces

6 interfaces between chains.

A–F · 759 Å² buried · 5 hydrogen bonds · protein-protein
C–D · 656 Å² buried · 6 hydrogen bonds · protein-protein
E–F · 293 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 143 Å² buried · 1 hydrogen bond · protein-protein
A–C · 113 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4CU5 · C-terminal domain of endolysin from phage CD27L is a trigger and release factor · 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 B6SBV8
Elsewhere: RCSB PDB 4CU5 · PDBe 4CU5 · UniProt B6SBV8

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