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Crystal structure of HIV-2 reverse transcriptase

Analyse Crystal structure of HIV-2 reverse transcriptase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MU2
Type: protein
Length: 940 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-2 rt
EC: 2.7.7.49
UniProt: P04584
Ligands: SO4
Pockets: 16 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	HIV-2 rt (EC 2.7.7.49)	protein	538	33% helix, 25% strand	P04584
B	HIV-2 rt (EC 2.7.7.49)	protein	402	38% helix, 20% strand	P04584

Ligands and binding sites

SO4 · Sulfate ion · ion · 22 copies · chains A, B
GOL · Glycerol · additive · 5 copies · chains A, B

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

Pockets

16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	635	0.72	0.79	72	empty
2	629	0.70	0.78	60	GOL
3	299	0.68	0.83	32	GOL
4	332	0.66	0.81	32	SO4, GOL
5	99	0.65	0.90	28	SO4

Interfaces

1 interface between chains.

A–B · 3063 Å² buried · 44 hydrogen bonds · protein-protein

Compared structures

1MU2 · Crystal structure of HIV-2 reverse transcriptase · 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 P04584
Elsewhere: RCSB PDB 1MU2 · PDBe 1MU2 · UniProt P04584

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