MolNFT v1 · #11960 · protein

Combining mutations in HIV-1 protease to understand mechanisms of resistance

1K2B · Protease retropepsin: “Combining mutations in HIV-1 protease to understand mechanisms of resistance”. X-ray diffraction, 1 ligand (0Q4), 1 pocket (best druggability 0.71). MolNFT v1 #11960 on GenesisL1: 3D structure, binding sites…

PDB: 1K2B
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease retropepsin
EC: 3.4.23.16
UniProt: P04587
Ligands: 0Q4
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease retropepsin (EC 3.4.23.16)	protein	99	4% helix, 58% strand	P04587

Ligands and binding sites

0Q4 · N-[(2R)-2-({N~5~-[amino(iminio)methyl]-L-ornithyl-L-valyl}amino)-4-methylpentyl]-L-phenylalanyl-L-alpha-glutamyl-L-alanyl-L-norleucinamide · ligand · 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	342	0.71	0.83	36	0Q4

Interfaces

1 interface between chains.

A–B · 1827 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

1K2B · Combining Mutations in HIV-1 Protease to Understand Mechanisms of Resistance · 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 P04587
Elsewhere: RCSB PDB 1K2B · PDBe 1K2B · UniProt P04587

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