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Structural genomics of C.ELEGANS: fkbp-type peptidylprolyl isomerase

Analyse Structural genomics of C.ELEGANS: fkbp-type peptidylprolyl isomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1R9H
Type: protein
Length: 118 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FK506 binding protein family
UniProt: O45418
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FK506 binding protein family	protein	118	12% helix, 41% strand	O45418

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.32	0.76	12	empty

Compared structures

1R9H · Structural Genomics of C.elegans: FKBP-type Peptidylprolyl Isomerase · 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 O45418
Elsewhere: RCSB PDB 1R9H · PDBe 1R9H · UniProt O45418

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