MolNFT v1 · #150100 · protein

Cyclophilin a complexed with tri-vector ligand 15.

6GJN · Peptidyl-prolyl cis-trans isomerase a: “Cyclophilin a complexed with tri-vector ligand 15.”. X-ray diffraction, 1 ligand (F0Q), 1 pocket (best druggability 0.32). MolNFT v1 #150100 on GenesisL1: 3D structure, binding sites and…

PDB: 6GJN
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: F0Q
Pockets: 1 · best druggability 0.32

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

F0Q · 1-[(4-aminophenyl)methyl]-3-[2-[(2~{R})-2-(2-bromophenyl)pyrrolidin-1-yl]-2-oxidanylidene-ethyl]-1-[(2-methyl-1,2,3,4-tetrazol-5-yl)methyl]urea · ligand · chains A
FMT · Formic acid · additive · 2 copies · 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	57	0.32	0.77	16	empty

Compared structures

6GJN · Cyclophilin A complexed with tri-vector ligand 15. · 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 6GJN · PDBe 6GJN · UniProt P62937

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