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Crystal structure of the N-terminal domain of NUP358/RANBP2 (residues 1-752) T585M mutant in complex with Fab fragment

Analyse Crystal structure of the N-terminal domain of NUP358/RANBP2 (residues 1-752)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7MNM
Type
protein
Length
2,228 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 sumo-protein ligase RANBP2; Antibody FAB14 heavy chain; Antibody FAB14 light chain
EC
2.3.2.-
UniProt
P49792
Pockets
20 · best druggability 0.81

Structure

x-ray diffraction · 4 distinct chains · 56% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE3 sumo-protein ligase RANBP2 (EC 2.3.2.-)protein74673% helix, 0% strandP49792
BE3 sumo-protein ligase RANBP2 (EC 2.3.2.-)protein60271% helix, 0% strandP49792
H, KAntibody FAB14 heavy chainprotein2277% helix, 52% strand—
L, MAntibody FAB14 light chainprotein2136% helix, 53% strand—

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17250.810.8561empty
210150.730.7695empty
36950.720.7986empty
45060.650.7756empty
55080.650.7752empty

Interfaces

5 interfaces between chains.

  • H–L · 1989 Ų buried · 16 hydrogen bonds · protein-protein
  • K–M · 1938 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 1073 Ų buried · 20 hydrogen bonds · protein-protein
  • A–H · 989 Ų buried · 14 hydrogen bonds · protein-protein
  • B–K · 823 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 7MNM · Crystal structure of the N-terminal domain of NUP358/RanBP2 (residues 1-752) T585M mutant… · the same entry in another collection · chain A against A, TM-score 1.00

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