MolNFT v1 · #150095 · protein

Cyclophilin a complexed with the tri-vector ligand 8.

6GJI · Peptidyl-prolyl cis-trans isomerase a: “Cyclophilin a complexed with the tri-vector ligand 8.”. X-ray diffraction, 1 ligand (F1E), 1 pocket (best druggability 0.29). MolNFT v1 #150095 on GenesisL1: 3D structure, binding sites and…

PDB: 6GJI
Type: protein
Length: 165 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase a
EC: 5.2.1.8
UniProt: P62937
Ligands: F1E
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8)	protein	165	14% helix, 34% strand	P62937

Ligands and binding sites

F1E · ethyl 2-[[(4-aminophenyl)methyl-[(1-methyl-1,2,3-triazol-4-yl)methyl]carbamoyl]amino]ethanoate · ligand · chains A
GOL · Glycerol · additive · chains A

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

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	58	0.29	0.75	16	empty

Compared structures

6GJI · Cyclophilin A complexed with the tri-vector ligand 8. · 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 6GJI · PDBe 6GJI · UniProt P62937

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