MolNFT v1 · #140059 · protein

Crystal structure of a serine protease from streptococcus species

5XYR · Chemokine protease C: “Crystal structure of a serine protease from streptococcus species”. X-ray diffraction, 3 ligands (CA, CL, SO4), 20 pockets (best druggability 0.73). MolNFT v1 #140059 on GenesisL1: 3D structure, binding sites…

PDB: 5XYR
Type: protein
Length: 1,380 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chemokine protease C
UniProt: Q3HV58
Ligands: CA, CL, SO4
Pockets: 20 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chemokine protease C	protein	1380	11% helix, 34% strand	Q3HV58

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A
CL · Chloride ion · ion · chains A
SO4 · Sulfate ion · ion · chains A
MLA · Malonic acid · additive · chains A

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

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1197	0.73	0.77	93	empty
2	670	0.73	0.80	78	MLA
3	50	0.71	0.99	25	empty
4	392	0.71	0.83	61	empty
5	253	0.68	0.84	29	empty

Modifications

Observed in the structure: 25 modified (engineered).

Compared structures

5XYR · Crystal structure of a serine protease from Streptococcus species · 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 Q3HV58
Elsewhere: RCSB PDB 5XYR · PDBe 5XYR · UniProt Q3HV58

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