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Human pepsin 3A in complex with a phosphonate inhibitor iva-val-val- LEU(P)-(O)PHE-ala-ala-ome

Analyse Human pepsin 3A in complex with a phosphonate inhibitor iva-val-val… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QRP
Type: protein
Length: 326 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pepsin 3A
UniProt: P00790
Ligands: HH0
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Pepsin 3A	protein	326	17% helix, 46% strand	P00790

Ligands and binding sites

HH0 · methyl N-[(2S)-2-({(S)-hydroxy[(1R)-3-methyl-1-{[N-(3-methylbutanoyl)-L-valyl-L-valyl]amino}butyl]phosphoryl}oxy)-3-phenylpropanoyl]-L-alanyl-L-alaninate · ligand · chains E

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	360	0.62	0.78	47	HH0
2	59	0.32	0.77	15	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1QRP · Human pepsin 3A in complex with a phosphonate inhibitor… · the same entry in another collection · chain E against E, 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 P00790
Elsewhere: RCSB PDB 1QRP · PDBe 1QRP · UniProt P00790

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