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Crystal structure of lugdulysin, a staphylococcus lugdunensis M30 zinc metallopeptidase

Analyse Crystal structure of lugdulysin, a staphylococcus lugdunensis M30 zinc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BB8
Type: protein
Length: 720 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neutral metalloprotease
UniProt: A0A292DHH8
Ligands: CA, ZN
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Neutral metalloprotease	protein	360	40% helix, 17% strand	A0A292DHH8

Ligands and binding sites

CA · Calcium ion · metal · 6 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B
CAC · Cacodylate ion · additive · chains A
ACT · Acetate ion · additive · chains B

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

Pockets

2 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	457	0.59	0.74	43	CAC
2	329	0.53	0.74	35	ACT

Compared structures

7BB8 · Crystal structure of Lugdulysin, a Staphylococcus lugdunensis M30 zinc metallopeptidase · 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 A0A292DHH8
Elsewhere: RCSB PDB 7BB8 · PDBe 7BB8 · UniProt A0A292DHH8

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