MolNFT v1 · #1274 · protein

Cypa complexed with hagpia

1AWR · Cyclophilin a: “Cypa complexed with hagpia”. X-ray diffraction, 6 pockets (best druggability 0.39). MolNFT v1 #1274 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1AWR
Type: protein
Length: 1,020 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclophilin a; Peptide from the HIV-1 capsid protein
EC: 5.2.1.8
UniProt: P62937
Pockets: 6 · best druggability 0.39

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Cyclophilin a (EC 5.2.1.8)	protein	164	15% helix, 31% strand	P62937
G, H, I, J, K, L	Peptide from the HIV-1 capsid protein	protein	6	0% helix, 0% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.39	0.80	16	empty
2	61	0.36	0.78	17	empty
3	68	0.35	0.77	17	empty
4	59	0.34	0.78	17	empty
5	63	0.33	0.77	17	empty

Interfaces

6 interfaces between chains.

D–J · 431 Å² buried · 7 hydrogen bonds · protein-protein
B–H · 430 Å² buried · 7 hydrogen bonds · protein-protein
C–I · 412 Å² buried · 7 hydrogen bonds · protein-protein
E–K · 393 Å² buried · 7 hydrogen bonds · protein-protein
A–G · 379 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1AWR · Cypa complexed with hagpia · the same entry in another collection · chain E against E, 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 1AWR · PDBe 1AWR · UniProt P62937

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