MolNFT v1 · #175068 · protein

Drosophila melanogaster krimper ETUD1-AGO3 complex

7CFC · FI20010P1: “Drosophila melanogaster krimper ETUD1-AGO3 complex”. X-ray diffraction, 10 pockets (best druggability 0.73). MolNFT v1 #175068 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7CFC
Type: protein
Length: 915 residues
Chains: 9
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FI20010P1; Protein argonaute-3
UniProt: A1ZAC4, Q7PLK0
Pockets: 10 · best druggability 0.73

Structure

x-ray diffraction · 6 distinct chains · 17% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	FI20010P1	protein	178	19% helix, 40% strand	A1ZAC4
C, D	FI20010P1	protein	179	16% helix, 41% strand	A1ZAC4
E	FI20010P1	protein	161	8% helix, 45% strand	A1ZAC4
F, G	Protein argonaute-3	protein	11	64% helix, 0% strand	Q7PLK0
H	Protein argonaute-3	protein	8	75% helix, 0% strand	Q7PLK0
I	Protein argonaute-3	protein	10	60% helix, 0% strand	Q7PLK0

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	726	0.73	0.79	65	empty
2	680	0.73	0.79	72	empty
3	351	0.61	0.77	39	empty
4	237	0.54	0.77	40	empty
5	163	0.46	0.76	23	empty

Interfaces

13 interfaces between chains.

D–I · 685 Å² buried · 9 hydrogen bonds · protein-protein
B–G · 631 Å² buried · 7 hydrogen bonds · protein-protein
A–F · 621 Å² buried · 7 hydrogen bonds · protein-protein
C–H · 575 Å² buried · 5 hydrogen bonds · protein-protein
B–C · 558 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

7CFC · Drosophila melanogaster Krimper eTud1-Ago3 complex · the same entry in another collection · chain I against I, TM-score 1.00
Q7PLK0 · AlphaFold monomer V2.0 prediction for protein argonaute-3 (Q7PLK0) · a predicted model of the same protein · chain H against A, TM-score 0.64

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 A1ZAC4
Every structure of UniProt Q7PLK0
Elsewhere: RCSB PDB 7CFC · PDBe 7CFC · UniProt A1ZAC4 · UniProt Q7PLK0

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