MolNFT v1 · #150104 · protein

Cyclophilin a complexed with tri-vector ligand 9.

6GJR · Peptidyl-prolyl cis-trans isomerase a: “Cyclophilin a complexed with tri-vector ligand 9.”. X-ray diffraction, 1 ligand (F0W), 1 pocket (best druggability 0.39). MolNFT v1 #150104 on GenesisL1: 3D structure, binding sites and…

PDB: 6GJR
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: F0W
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 33% 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, 33% strand	P62937

Ligands and binding sites

F0W · ethyl 2-[[(4-aminophenyl)methyl-[(2-methyl-1,2,3,4-tetrazol-5-yl)methyl]carbamoyl]amino]ethanoate · ligand · 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	85	0.39	0.77	23	F0W

Compared structures

6GJR · Cyclophilin A complexed with tri-vector ligand 9. · 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 6GJR · PDBe 6GJR · UniProt P62937

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