MolNFT v1 · #169198 · protein
Human cyclophilin a bound to a series of acylcic and macrocyclic inhibitors
6X3Y · Peptidyl-prolyl cis-trans isomerase a: “Human cyclophilin a bound to a series of acylcic and macrocyclic inhibitors”. X-ray diffraction, 1 ligand (UMM). MolNFT v1 #169198 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6X3Y
- Type
- protein
- Length
- 166 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
- UMM
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8) | protein | 166 | 14% helix, 31% strand | P62937 |
Ligands and binding sites
- UMM · Tert-butyl [(2S)-1-{[(3S,17S)-2,16-dioxo-10,15-dioxa-1, 21-diazatricyclo[15.3.1.1~5,9~]docosa-5(22),6,8-trien-3-yl]amino}-3-methyl-1-oxobutan-2-yl]carbamate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6X3Y · Human cyclophilin A bound to a series of acylcic and macrocyclic inhibitors · 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 6X3Y · PDBe 6X3Y · UniProt P62937
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