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Crystal structure of the 50 kda metallo protease from S. marcescens

Analyse Crystal structure of the 50 kda metallo protease from S. marcescens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SAT
Type: protein
Length: 468 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serratia protease
UniProt: P23694
Ligands: CA, ZN
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serratia protease	protein	468	18% helix, 24% strand	P23694

Ligands and binding sites

CA · Calcium ion · metal · 7 copies · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

3 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	125	0.47	0.79	20	empty
2	103	0.38	0.75	17	empty
3	102	0.32	0.72	17	empty

Compared structures

1SAT · Crystal structure of the 50 kda metallo protease from S. marcescens · the same entry in another collection · chain A against A, TM-score 1.00
P23694 · AlphaFold monomer V2.0 prediction for serralysin (P23694) · a predicted model of the same protein · 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 P23694
Elsewhere: RCSB PDB 1SAT · PDBe 1SAT · UniProt P23694

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