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Complex of rabbit endogenous lentivirus (RELIK)CAPSID with cyclophilin a

Analyse Complex of rabbit endogenous lentivirus (RELIK)CAPSID with cyclophilin a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XGY
Type: protein
Length: 294 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Relik capsid N-terminal domain; Peptidyl-prolyl cis-trans isomerase a
EC: 5.2.1.8
UniProt: P62937
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Relik capsid N-terminal domain	protein	129	63% helix, 2% strand	—
B	Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8)	protein	165	14% helix, 32% strand	P62937

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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	82	0.40	0.78	22	GOL
2	66	0.39	0.80	18	empty

Interfaces

1 interface between chains.

A–B · 781 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

2XGY · Complex of Rabbit Endogenous Lentivirus (RELIK)Capsid with Cyclophilin A · 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 P62937
Elsewhere: RCSB PDB 2XGY · PDBe 2XGY · UniProt P62937

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