Research workbench

Cypa complexed with hvgpia

Analyse Cypa complexed with hvgpia in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AWV
Type: protein
Length: 1,020 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclophilin a; Peptide from the HIV-1 capsid protein
EC: 5.2.1.8
UniProt: P62937
Pockets: 5 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Cyclophilin a (EC 5.2.1.8)	protein	164	13% helix, 34% strand	P62937
G, H, I, J, K, L	Peptide from the HIV-1 capsid protein	protein	6	0% helix, 0% strand	—

Pockets

5 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	61	0.35	0.78	17	empty
2	59	0.35	0.78	17	empty
3	57	0.34	0.77	15	empty
4	53	0.34	0.78	15	empty
5	51	0.31	0.77	15	empty

Interfaces

6 interfaces between chains.

C–I · 441 Å² buried · 7 hydrogen bonds · protein-protein
D–J · 424 Å² buried · 6 hydrogen bonds · protein-protein
E–K · 421 Å² buried · 6 hydrogen bonds · protein-protein
B–H · 407 Å² buried · 6 hydrogen bonds · protein-protein
F–L · 404 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1AWV · Cypa complexed with hvgpia · the same entry in another collection · chain C against C, 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 P62937
Elsewhere: RCSB PDB 1AWV · PDBe 1AWV · UniProt P62937

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