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HIV-1 protease (I84V) in complex with PU5 (LR4-47)

Analyse HIV-1 protease (I84V) in complex with PU5 (LR4-47) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MAI
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
EC: 3.4.23.16
UniProt: P03367
Ligands: XVJ
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Protease (EC 3.4.23.16)	protein	99	7% helix, 55% strand	P03367

Ligands and binding sites

XVJ · Diethyl [(4-{(2S,3R)-4-{[(1,3-benzothiazol-6-yl) sulfonyl][(2s)-2-methylbutyl]amino}-2-[({[(3r,3as, 6AR)-hexahydrofuro[2,3-b]furan-3-yl]oxy}carbonyl) amino]-3-hydroxybutyl}phenoxy)methyl]phosphonate · ligand · chains B, 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	385	0.71	0.82	33	XVJ

Interfaces

1 interface between chains.

B–A · 1802 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

7MAI · HIV-1 Protease (I84V) in Complex with PU5 (LR4-47) · the same entry in another collection · chain B against B, 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 P03367
Elsewhere: RCSB PDB 7MAI · PDBe 7MAI · UniProt P03367

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