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Structure of the wild-type native full-length HIV-1 capsid protein in complex with zw-1261

Analyse Structure of the wild-type native full-length HIV-1 capsid protein in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7M9F
Type: protein
Length: 221 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 capsid protein
UniProt: P12493
Ligands: YTG, IOD
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	HIV-1 capsid protein	protein	221	57% helix, 3% strand	P12493

Ligands and binding sites

YTG · N-(4-chlorophenyl)-nalpha-[(5-hydroxy-1H-indol-3-yl) acetyl]-N-methyl-L-phenylalaninamide · ligand · chains A
IOD · Iodide ion · ion · 5 copies · chains A

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

Pockets

2 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	83	0.36	0.76	16	YTG
2	76	0.33	0.74	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7M9F · Structure of the wild-type native full-length HIV-1 capsid protein in complex with ZW-1261 · 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 7M9F · PDBe 7M9F · UniProt P12493

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