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Substrate shape determines specificity of recognition recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes

Analyse Substrate shape determines specificity of recognition recognition for HIV-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KJ7
Type: protein
Length: 206 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pol polyprotein; Gag polyprotein
EC: 3.4.23.16
UniProt: P03369, P20875

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pol polyprotein (EC 3.4.23.16)	protein	99	7% helix, 55% strand	P03369
P	Gag polyprotein	protein	8	0% helix, 50% strand	P20875

Ligands and binding sites

ACT · Acetate ion · additive · 5 copies · chains A, B

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

Interfaces

3 interfaces between chains.

A–B · 1847 Å² buried · 37 hydrogen bonds · protein-protein
A–P · 528 Å² buried · 6 hydrogen bonds · protein-protein
B–P · 505 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1KJ7 · Substrate shape determines specificity of recognition recognition for HIV-1 protease… · 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 P03369
Every structure of UniProt P20875
Elsewhere: RCSB PDB 1KJ7 · PDBe 1KJ7 · UniProt P03369 · UniProt P20875

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