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X-ray Snapshot of HIV-1 Protease in Action: Observation of Tetrahedral Intermediate and Its SIHB with Catalytic Aspartate

Analyse X-ray Snapshot of HIV-1 Protease in Action: Observation of Tetrahedral… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YRS
Type: protein
Length: 208 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.76
Source: Human immunodeficiency virus 1; SYNTHETIC CONSTRUCT
Molecule: Protease; RT-RH oligopeprtide
EC: 3.4.23.16
UniProt: P04585

Structure

x-ray diffraction · resolution 1.76 · 3 distinct chains · 7% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protease (EC 3.4.23.16)	protein	99	7% helix, 56% strand	P04585
B	Protease (EC 3.4.23.16)	protein	103	7% helix, 53% strand	P04585
X	RT-RH oligopeprtide	protein	6	0% helix, 33% strand	—

Interfaces

3 interfaces between chains.

A–B · 1936 Å² buried · 41 hydrogen bonds · protein-protein
B–X · 492 Å² buried · 8 hydrogen bonds · protein-protein
A–X · 449 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

5YRS · X-ray snapshot of HIV-1 protease in action: observation of tetrahedral intermediate and… · 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 P04585
Elsewhere: RCSB PDB 5YRS · PDBe 5YRS · UniProt P04585

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