MolNFT v1 · #160056 · protein

HIV-1 protease multiple drug resistant mutant PRS5B with amprenavir

6P9B: “HIV-1 protease multiple drug resistant mutant PRS5B with amprenavir”. X-ray diffraction, 2 ligands (478, PO4), 1 pocket (best druggability 0.74). MolNFT v1 #160056 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6P9B
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 protease
EC: 3.4.23.16
UniProt: P03367
Ligands: 478, PO4
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	HIV-1 protease (EC 3.4.23.16)	protein	99	6% helix, 54% strand	P03367

Ligands and binding sites

478 · {3-[(4-amino-benzenesulfonyl)-isobutyl-amino]-1-benzyl-2-hydroxy-propyl}-carbamic acid tetrahydro-furan-3-yl ester · ligand · chains A, B
PO4 · Phosphate ion · ion · 4 copies · chains A, B

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	366	0.74	0.85	39	478, PO4

Interfaces

1 interface between chains.

A–B · 1847 Å² buried · 38 hydrogen bonds · protein-protein

Compared structures

6P9B · HIV-1 Protease multiple drug resistant mutant PRS5B with Amprenavir · 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 P03367
Elsewhere: RCSB PDB 6P9B · PDBe 6P9B · UniProt P03367

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