Research workbench

Crystal structure of the putative NLPC/P60 D,L endopeptidase from T. thermophilus

Analyse Crystal structure of the putative NLPC/P60 D,L endopeptidase from T.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XCM
Type: protein
Length: 393 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell wall-binding endopeptidase-related protein
UniProt: Q5SLM7
Pockets: 4 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell wall-binding endopeptidase-related protein	protein	175	29% helix, 21% strand	Q5SLM7
B	Cell wall-binding endopeptidase-related protein	protein	218	27% helix, 20% strand	Q5SLM7

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	96	0.41	0.77	21	empty
2	89	0.36	0.75	19	empty
3	51	0.32	0.77	11	empty
4	52	0.27	0.74	11	empty

Interfaces

1 interface between chains.

A–B · 2237 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

4XCM · Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus · 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 Q5SLM7
Elsewhere: RCSB PDB 4XCM · PDBe 4XCM · UniProt Q5SLM7

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.