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Crystal structure of fkbp from plasmodium vivax in complex with tetrapeptide alpf

Analyse Crystal structure of fkbp from plasmodium vivax in complex with tetrapeptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PA7
Type: protein
Length: 251 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 70 kda peptidylprolyl isomerase, putative; 4-mer peptide alpf
EC: 5.2.1.8
UniProt: A5K8X6
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 3 distinct chains · 14% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	70 kda peptidylprolyl isomerase, putative (EC 5.2.1.8)	protein	124	15% helix, 38% strand	A5K8X6
B	70 kda peptidylprolyl isomerase, putative (EC 5.2.1.8)	protein	123	15% helix, 38% strand	A5K8X6
D	4-mer peptide alpf	protein	4	0% helix, 0% strand	—

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	403	0.58	0.75	45	empty

Interfaces

2 interfaces between chains.

A–B · 326 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 240 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

3PA7 · Crystal structure of FKBP from plasmodium vivax in complex with tetrapeptide ALPF · the same entry in another collection · chain B against B, 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 3PA7 · PDBe 3PA7 · UniProt A5K8X6

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