MolNFT v1 · #126859 · protein

Designed armadillo repeat protein YIII(DQ.V2)4CQI in complex with peptide (KR)5

5MFJ: “Designed armadillo repeat protein YIII(DQ.V2)4CQI in complex with peptide (KR)5”. X-ray diffraction, 3 pockets (best druggability 0.76). MolNFT v1 #126859 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5MFJ
Type: protein
Length: 495 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: YIII(DQ.V2)4CQI; (KR)5
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 4 distinct chains · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	YIII(DQ.V2)4CQI	protein	239	77% helix, 0% strand	—
B	YIII(DQ.V2)4CQI	protein	240	75% helix, 0% strand	—
C	(KR)5	protein	6	0% helix, 0% strand	—
D	(KR)5	protein	10	0% helix, 0% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	797	0.76	0.80	85	empty
2	88	0.33	0.74	15	empty
3	52	0.27	0.74	14	empty

Interfaces

5 interfaces between chains.

A–D · 721 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 570 Å² buried · 4 hydrogen bonds · protein-protein
B–D · 510 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 448 Å² buried · 13 hydrogen bonds · protein-protein
C–D · 116 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5MFJ · Designed armadillo repeat protein YIII(Dq.V2)4CqI in complex with peptide (KR)5 · 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
Elsewhere: RCSB PDB 5MFJ · PDBe 5MFJ

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.