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Evolutionary basis of HIV restriction by the antiretroviral trimcyp

Analyse Evolutionary basis of HIV restriction by the antiretroviral trimcyp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X82
Type: protein
Length: 580 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein P24
Pockets: 6 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Capsid protein P24	protein	145	56% helix, 4% strand	—

Pockets

6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.38	0.81	13	empty
2	68	0.36	0.77	13	empty
3	56	0.28	0.75	13	empty
4	76	0.28	0.72	16	empty
5	65	0.28	0.73	8	empty

Interfaces

4 interfaces between chains.

C–D · 806 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 780 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 527 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 57 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2X82 · Evolutionary basis of HIV restriction by the antiretroviral TRIMCyp · 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
Elsewhere: RCSB PDB 2X82 · PDBe 2X82

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