Research workbench

An atomic model of HIV-1 ca-SP1 reveals structures regulating assembly and maturation

Analyse An atomic model of HIV-1 ca-SP1 reveals structures regulating assembly and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5L93
Type: protein
Length: 672 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein P24
UniProt: P12493
Pockets: 13 · best druggability 0.74

Structure

electron microscopy · 1 distinct chain · 63% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Capsid protein P24	protein	224	63% helix, 0% strand	P12493

Pockets

13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	974	0.74	0.77	86	empty
2	57	0.72	0.98	23	empty
3	53	0.70	0.97	18	empty
4	130	0.66	0.88	22	empty
5	237	0.52	0.76	28	empty

Interfaces

3 interfaces between chains.

A–B · 1104 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 1081 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 674 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

5L93 · An atomic model of HIV-1 CA-SP1 reveals structures regulating assembly and maturation · 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 P12493
Elsewhere: RCSB PDB 5L93 · PDBe 5L93 · UniProt P12493

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.