MolNFT v1 · #36434 · protein

Crystal structure of mrg domain from human MRG15

2F5J · Mortality factor 4-like protein 1: “Crystal structure of mrg domain from human MRG15”. X-ray diffraction, 4 pockets (best druggability 0.71). MolNFT v1 #36434 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2F5J
Type: protein
Length: 316 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mortality factor 4-like protein 1
UniProt: Q9UBU8
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mortality factor 4-like protein 1	protein	157	71% helix, 5% strand	Q9UBU8
B	Mortality factor 4-like protein 1	protein	159	70% helix, 5% strand	Q9UBU8

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	104	0.71	0.93	20	empty
2	410	0.59	0.75	44	empty
3	92	0.37	0.75	16	empty
4	57	0.29	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 1179 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2F5J · Crystal structure of MRG domain from human MRG15 · the same entry in another collection · chain A against A, TM-score 1.00
Q9UBU8 · AlphaFold monomer V2.0 prediction for mortality factor 4-like protein 1 (Q9UBU8) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9UBU8
Elsewhere: RCSB PDB 2F5J · PDBe 2F5J · UniProt Q9UBU8

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