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The crystal structure of rhodesain, the major cysteine protease of T. brucei rhodesiense, bound to inhibitor K777

Analyse The crystal structure of rhodesain, the major cysteine protease of T. brucei… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P7U
Type: protein
Length: 215 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine protease
UniProt: Q95PM0
Ligands: D1R
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cysteine protease	protein	215	28% helix, 23% strand	Q95PM0

Ligands and binding sites

D1R · Nalpha-[(4-methylpiperazin-1-yl)carbonyl]-N-{(1S)-3-phenyl-1-[2-(phenylsulfonyl)ethyl]propyl}-L-phenylalaninamide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	67	0.30	0.74	17	empty

Modifications

Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

2P7U · The crystal structure of rhodesain, the major cysteine protease of T. brucei rhodesiense… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt Q95PM0
Elsewhere: RCSB PDB 2P7U · PDBe 2P7U · UniProt Q95PM0

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