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Crystal structure of the FK506 binding domain of plasmodium vivax FKBP35

Analyse Crystal structure of the FK506 binding domain of plasmodium vivax FKBP35 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NI6
Type: protein
Length: 245 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 70 kda peptidylprolyl isomerase
UniProt: A5K8X6
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	70 kda peptidylprolyl isomerase	protein	124	12% helix, 37% strand	A5K8X6
B	70 kda peptidylprolyl isomerase	protein	121	12% helix, 39% strand	A5K8X6

Ligands and binding sites

GOL · Glycerol · additive · 8 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	944	0.77	0.79	60	GOL

Interfaces

1 interface between chains.

A–B · 557 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3NI6 · Crystal structure of the FK506 binding domain of Plasmodium vivax FKBP35 · 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 A5K8X6
Elsewhere: RCSB PDB 3NI6 · PDBe 3NI6 · UniProt A5K8X6

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