Research workbench

Crystal structure of the N-terminal domain of NUP358/RANBP2 (residues 145-673)

Analyse Crystal structure of the N-terminal domain of NUP358/RANBP2 (residues 145-673) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MNJ
Type: protein
Length: 1,586 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 sumo-protein ligase RANBP2
EC: 2.3.2.-
UniProt: P49792
Pockets: 20 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	E3 sumo-protein ligase RANBP2 (EC 2.3.2.-)	protein	529	71% helix, 0% strand	P49792
C	E3 sumo-protein ligase RANBP2 (EC 2.3.2.-)	protein	528	72% helix, 0% strand	P49792

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	449	0.79	0.87	53	empty
2	956	0.78	0.80	86	empty
3	304	0.75	0.87	43	empty
4	791	0.74	0.79	82	empty
5	183	0.67	0.86	29	empty

Interfaces

2 interfaces between chains.

B–C · 2403 Å² buried · 20 hydrogen bonds · protein-protein
A–B · 2230 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

7MNJ · Crystal structure of the N-terminal domain of NUP358/RanBP2 (residues 145-673) · 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 P49792
Elsewhere: RCSB PDB 7MNJ · PDBe 7MNJ · UniProt P49792

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