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HIV-1 reverse transcriptase rh domain

Analyse HIV-1 reverse transcriptase rh domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DZM
Type: protein
Length: 454 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease H
EC: 3.1.26.4
UniProt: Q7LYY8
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Ribonuclease H (EC 3.1.26.4)	protein	115	35% helix, 30% strand	Q7LYY8
D, B	Ribonuclease H (EC 3.1.26.4)	protein	112	34% helix, 31% strand	Q7LYY8

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	1105	0.76	0.79	79	empty

Interfaces

6 interfaces between chains.

D–C · 2812 Å² buried · 35 hydrogen bonds · protein-protein
A–B · 2810 Å² buried · 36 hydrogen bonds · protein-protein
D–B · 738 Å² buried · 4 hydrogen bonds · protein-protein
C–B · 582 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 579 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5DZM · HIV-1 Reverse Transcriptase RH domain · 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 Q7LYY8
Elsewhere: RCSB PDB 5DZM · PDBe 5DZM · UniProt Q7LYY8

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